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secD secD secA secA secF secF yajR yajR cyoD cyoD cyoC cyoC cyoB cyoB cyoA cyoA tolR tolR tolA tolA msbA msbA cysU cysU emrE emrE secE secE yrbK yrbK secG secG atpB atpB atpE atpE atpF atpF atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC pitA pitA corA corA yjcE yjcE gltP gltP tonB tonB manX manX mviN mviN yceL yceL omp omp nuoN nuoN nuoM nuoM nuoL nuoL nuoJ nuoJ nuoG nuoG nuoF nuoF nuoCD nuoCD nuoB nuoB nuoA nuoA mntH mntH nupC nupC cysA cysA cysW cysW
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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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
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secDPreprotein translocase, auxillary membrane component; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (619 aa)
secAPreprotein translocase, ATPase secretion component; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. (911 aa)
secFPreprotein translocase, auxillary membrane component; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (305 aa)
yajRPutative transport protein (MFS family); Ortholog to Escherichia coli bnum: b0427; MultiFun: Cell processes 5.6.4; Cell structure 6.1; Transport 4.2.A.1,4.S.49. (386 aa)
cyoDCytochrome o ubiquinol oxidase, subunit IV; Ortholog to Escherichia coli bnum: b0429; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.4.2. (100 aa)
cyoCCytochrome o ubiquinol oxidase, subunit III; Ortholog to Escherichia coli bnum: b0430; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.4.2; Transport 4.3.D.4, 4.S.82. (195 aa)
cyoBCytochrome o ubiquinol oxidase, subunit I; Ortholog to Escherichia coli bnum: b0431; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.4.2; Transport 4.3.D.4, 4.S.82; Belongs to the heme-copper respiratory oxidase family. (653 aa)
cyoACytochrome o ubiquinol oxidase, subunit II; Ortholog to Escherichia coli bnum: b0432; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.4.2; Transport 4.3.D.4, 4.S.82. (294 aa)
tolRTolR; Role in outer membrane integrity, uptake of group A colicins (TonB-independent), and phage DNA; ortholog to Escherichia coli bnum: b0738; MultiFun: Cell structure 6.1. (141 aa)
tolATolA; Required for outer membrane integrity, uptake of group A colicins, role in translocation of filamenous phage DNA to cytoplasm, role in surface expression of O-antigen; ortholog to Escherichia coli bnum: b0739; MultiFun: Cell structure 6.1; Metabolism 1.6.3.1. (394 aa)
msbALipid transport protein; Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. (584 aa)
cysUThiosulfate transport protein (ABC superfamily, membrane); Part of the ABC transporter complex (TC 3.A.1.6.1) involved in sulfate/thiosulfate import; Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily. (277 aa)
emrEAuxillary multidrug transport protein (SMR family); Ortholog to Escherichia coli bnum: b0543; MultiFun: Cell processes 5.6.4; Cell structure 6.1; Transport 4.2.A.7, 4.S.126. (109 aa)
secEPreprotein translocase, membrane component; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation; Belongs to the SecE/SEC61-gamma family. (115 aa)
yrbKPossible exported protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. (205 aa)
secGPreprotein translocase, membrane component; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. (93 aa)
atpBATP synthase, F0 sector, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (269 aa)
atpEATP synthase, F0 sector, subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (79 aa)
atpFATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (160 aa)
atpHATP synthase, F1 sector, delta-subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. (181 aa)
atpAATP synthase, F1 sector, alpha-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family. (513 aa)
atpGATP synthase, F1 sector, gamma-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (288 aa)
atpDATP synthase, F1 sector, beta-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (462 aa)
atpCATP synthase, F1 sector, epsilon-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (144 aa)
pitALow-affinity phosphate transport protein (PiT family); Ortholog to Escherichia coli bnum: b3493; MultiFun: Cell structure 6.1; Metabolism 1.8.1; Transport 4.2.A.20, 4.S.155. (540 aa)
corAMg2+/Ni2+/Co2+ transport protein (Mg transport system I) (MIT family); Mediates influx of magnesium ions. Can also mediate cobalt and manganese uptake (By similarity). Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high (By similarity). Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family. (314 aa)
yjcEPutative sodium:hydrogen antiporter (CPA1 family); Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons; Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. (547 aa)
gltPGlutamate:aspartate symporter (DAACS family); Catalyzes the proton-dependent transport of glutamate and aspartate; Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family. GltP subfamily. (429 aa)
tonBEnergy transducer; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Belongs to the TonB family. (242 aa)
manXPTS family enzyme IIA/enzyme IIB, mannose-specific; Ortholog to Escherichia coli bnum: b1817; MultiFun: Metabolism 1.1.1; Transport 4.4.A.6, 4.S.116. (327 aa)
mviNPutative virulence factor; Involved in peptidoglycan biosynthesis. Transports lipid- linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. (515 aa)
yceLPutative membrane transporter (MFS family); Ortholog to Escherichia coli bnum: b1065; MultiFun: Cell processes 5.6.4; Cell structure 6.1; Transport 4.2.A.1, 4.S.126. (407 aa)
ompOuter membrane protein; Ortholog to Escherichia coli bnum: b2215; MultiFun: Cell structure 6.1; Transport 4.1.B.1, 4.S.92. (373 aa)
nuoNNADH dehydrogenase I chain N, membrane subunit; 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. (497 aa)
nuoMNADH dehydrogenase I chain M, membrane subunit; Ortholog to Escherichia coli bnum: b2277; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.3.7, 1.4.1; Transport 4.3.D.1, 4.S.130. (513 aa)
nuoLNADH dehydrogenase I chain L, membrane subunit; Ortholog to Escherichia coli bnum: b2278; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.3.7, 1.4.1; Transport 4.3.D.1, 4.S.130. (628 aa)
nuoJNADH dehydrogenase I chain 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. (183 aa)
nuoGNADH dehydrogenase I chain G; 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. (919 aa)
nuoFNADH dehydrogenase I chain F; 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. (443 aa)
nuoCDNADH dehydrogenase I chain C, D; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (596 aa)
nuoBNADH dehydrogenase I chain B, binds FeS cluster N2; 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. (236 aa)
nuoANADH dehydrogenase I chain 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. (146 aa)
mntHManganese/divalent cation transport protein (NRAMP family); H(+)-stimulated, divalent metal cation uptake system. Belongs to the NRAMP family. (411 aa)
nupCNucleoside transport protein (NUP family); Ortholog to Escherichia coli bnum: b2393; MultiFun: Cell structure 6.1; Metabolism 1.7.33; Transport 4.2.A.41, 4.S.146. (396 aa)
cysASulfate permease A protein, chromate resistance (ABC superfamily, atp_bind); Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system. (355 aa)
cysWThiosulfate permease W protein (ABC superfamily, membrane); Ortholog to Escherichia coli bnum: b2423; MultiFun: Cell structure 6.1; Metabolism 1.8.2; Transport 4.3.A.1.m, 4.S.178. (286 aa)
Your Current Organism:
Blochmannia pennsylvanicus
NCBI taxonomy Id: 291272
Other names: C. Blochmannia pennsylvanicus str. BPEN, Candidatus Blochmannia pennsylvanicus BPEN, Candidatus Blochmannia pennsylvanicus str. BPEN, Candidatus Blochmannia pennsylvanicus strain BPEN
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