STRINGSTRING
AOB29450.1 AOB29450.1 ctaB ctaB AOB29452.1 AOB29452.1 AOB33285.1 AOB33285.1 AOB29453.1 AOB29453.1 AOB29454.1 AOB29454.1 AOB29455.1 AOB29455.1 AOB29457.1 AOB29457.1 AOB29458.1 AOB29458.1 AOB29475.1 AOB29475.1 AOB29503.1 AOB29503.1 AOB29504.1 AOB29504.1 AOB29505.1 AOB29505.1 AOB29632.1 AOB29632.1 AOB33315.1 AOB33315.1 AOB29805.1 AOB29805.1 AOB30162.1 AOB30162.1 AOB30233.1 AOB30233.1 AOB30234.1 AOB30234.1 AOB30235.1 AOB30235.1 AOB30236.1 AOB30236.1 AOB30237.1 AOB30237.1 AOB30238.1 AOB30238.1 AOB30438.1 AOB30438.1 AOB30439.1 AOB30439.1 AOB33471.1 AOB33471.1 AOB33472.1 AOB33472.1 AOB33473.1 AOB33473.1 AOB33474.1 AOB33474.1 AOB30518.1 AOB30518.1 msrP msrP AOB31341.1 AOB31341.1 AOB31412.1 AOB31412.1 AOB31413.1 AOB31413.1 AOB33697.1 AOB33697.1 AOB31414.1 AOB31414.1 AOB31415.1 AOB31415.1 AOB31416.1 AOB31416.1 AOB31417.1 AOB31417.1 AOB31418.1 AOB31418.1 AOB31460.1 AOB31460.1 AOB31461.1 AOB31461.1 AOB31462.1 AOB31462.1 AOB31463.1 AOB31463.1 AOB31464.1 AOB31464.1 AOB31465.1 AOB31465.1 AOB33709.1 AOB33709.1 AOB33710.1 AOB33710.1 AOB33711.1 AOB33711.1 AOB31466.1 AOB31466.1 AOB31912.1 AOB31912.1 nuoN nuoN AOB32191.1 AOB32191.1 AOB32192.1 AOB32192.1 nuoK nuoK AOB32194.1 AOB32194.1 nuoI nuoI nuoH nuoH AOB32197.1 AOB32197.1 AOB32198.1 AOB32198.1 AOB32199.1 AOB32199.1 nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA AOB33846.1 AOB33846.1 AOB32300.1 AOB32300.1 AOB32301.1 AOB32301.1 AOB32302.1 AOB32302.1 AOB32303.1 AOB32303.1 AOB33847.1 AOB33847.1 AOB33848.1 AOB33848.1 AOB32304.1 AOB32304.1 AOB33857.1 AOB33857.1 AOB32351.1 AOB32351.1 AOB32356.1 AOB32356.1 AOB32479.1 AOB32479.1 lgt lgt AOB32644.1 AOB32644.1 AOB32645.1 AOB32645.1 AOB32646.1 AOB32646.1 AOB32882.1 AOB32882.1 AOB33038.1 AOB33038.1 AOB34006.1 AOB34006.1
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
AOB29450.1Photosynthetic protein synthase I; Derived by automated computational analysis using gene prediction method: Protein Homology. (201 aa)
ctaBProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (297 aa)
AOB29452.1Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (347 aa)
AOB33285.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (215 aa)
AOB29453.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (252 aa)
AOB29454.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (66 aa)
AOB29455.1MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. (291 aa)
AOB29457.1Cytochrome oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (537 aa)
AOB29458.1Cytochrome C oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (386 aa)
AOB29475.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (213 aa)
AOB29503.1Ubiquinol-cytochrome C reductase; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (206 aa)
AOB29504.1Cytochrome B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (462 aa)
AOB29505.1Derived by automated computational analysis using gene prediction method: Protein Homology. (282 aa)
AOB29632.1Derived by automated computational analysis using gene prediction method: Protein Homology. (247 aa)
AOB33315.1Alcohol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (431 aa)
AOB29805.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (83 aa)
AOB30162.1NAD-dependent dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. (310 aa)
AOB30233.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (195 aa)
AOB30234.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (209 aa)
AOB30235.1Cytochrome C oxidase Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. (203 aa)
AOB30236.1Cytochrome C oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (199 aa)
AOB30237.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (546 aa)
AOB30238.1Alkyl hydroperoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (178 aa)
AOB30438.1Sir2 family NAD-dependent protein deacetylase; Derived by automated computational analysis using gene prediction method: Protein Homology. (286 aa)
AOB30439.1Beta-lactamase; Derived by automated computational analysis using gene prediction method: Protein Homology. (288 aa)
AOB33471.1Alcohol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (446 aa)
AOB33472.1Cytochrome C oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (198 aa)
AOB33473.1Cytochrome C oxidase; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (634 aa)
AOB33474.1Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (312 aa)
AOB30518.1Cytochrome oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (539 aa)
msrPSulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] (321 aa)
AOB31341.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (160 aa)
AOB31412.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (278 aa)
AOB31413.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (330 aa)
AOB33697.1Cytochrome C oxidase Cbb3; CcoN; FixN; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (499 aa)
AOB31414.1Peptidase S41; Derived by automated computational analysis using gene prediction method: Protein Homology. (219 aa)
AOB31415.1Cytochrome oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (58 aa)
AOB31416.1Cytochrome oxidase subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (326 aa)
AOB31417.1Cytochrome C oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (492 aa)
AOB31418.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (85 aa)
AOB31460.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (113 aa)
AOB31461.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (210 aa)
AOB31462.1Cytochrome C oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (530 aa)
AOB31463.1Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (315 aa)
AOB31464.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (279 aa)
AOB31465.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (105 aa)
AOB33709.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (205 aa)
AOB33710.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (174 aa)
AOB33711.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1006 aa)
AOB31466.1Derived by automated computational analysis using gene prediction method: Protein Homology. (216 aa)
AOB31912.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (175 aa)
nuoNNADH:ubiquinone oxidoreductase subunit N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (489 aa)
AOB32191.1NADH:ubiquinone oxidoreductase subunit M; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (495 aa)
AOB32192.1NADH:ubiquinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (684 aa)
nuoKNADH-quinone oxidoreductase subunit K; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (102 aa)
AOB32194.1NADH:ubiquinone oxidoreductase subunit J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (214 aa)
nuoINADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (162 aa)
nuoHNADH:ubiquinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (357 aa)
AOB32197.1NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. (775 aa)
AOB32198.1NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (455 aa)
AOB32199.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (164 aa)
nuoDNADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. (418 aa)
nuoCNADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family. (209 aa)
nuoBNADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (159 aa)
nuoANADH:ubiquinone oxidoreductase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. (119 aa)
AOB33846.1Arabinose ABC transporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology. (426 aa)
AOB32300.1Cytochrome O ubiquinol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (358 aa)
AOB32301.1Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (669 aa)
AOB32302.1Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (213 aa)
AOB32303.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (135 aa)
AOB33847.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (246 aa)
AOB33848.1Histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (452 aa)
AOB32304.1Chemotaxis protein CheY; Derived by automated computational analysis using gene prediction method: Protein Homology. (183 aa)
AOB33857.1Cytochrome; Derived by automated computational analysis using gene prediction method: Protein Homology. (120 aa)
AOB32351.1Derived by automated computational analysis using gene prediction method: Protein Homology. (115 aa)
AOB32356.1Zinc protease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M16 family. (916 aa)
AOB32479.1Derived by automated computational analysis using gene prediction method: Protein Homology. (117 aa)
lgtProlipoprotein diacylglyceryl transferase; Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins; Belongs to the Lgt family. (263 aa)
AOB32644.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (398 aa)
AOB32645.1Sulfite oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (420 aa)
AOB32646.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (108 aa)
AOB32882.1Derived by automated computational analysis using gene prediction method: Protein Homology. (302 aa)
AOB33038.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (176 aa)
AOB34006.1Derived by automated computational analysis using gene prediction method: Protein Homology. (226 aa)
Your Current Organism:
Bordetella sp. H567
NCBI taxonomy Id: 1697043
Other names: B. sp. H567
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