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nuoI nuoI nuoH nuoH nuoB nuoB nuoA nuoA yfbQ yfbQ fljB fljB rbfA rbfA frdB frdB yidC yidC yhbG yhbG secG secG dnaK dnaK murG murG glnD glnD proS proS STM0353 STM0353 flgB flgB flgC flgC flgK flgK flgL flgL pheT pheT galU galU argS argS motB motB fliA fliA fliC fliC fliH fliH fliK fliK fliM fliM nuoN nuoN nuoM nuoM nuoK nuoK
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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
protein homology
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nuoINADH dehydrogenase I chain I; 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. (180 aa)
nuoHNADH dehydrogenase I chain 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. (325 aa)
nuoBNADH dehydrogenase I chain B; 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. (220 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. (147 aa)
yfbQPutative regulator; similar to E. coli putative aminotransferase (AAC75350.1); Blastp hit to AAC75350.1 (405 aa), 96% identity in aa 1 - 404. (404 aa)
fljBFilament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (506 aa)
rbfARibosome-binding factor; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. (133 aa)
frdBFumarate reductase; Anaerobic; Fe-S protein subunit; similar to E. coli fumarate reductase, anaerobic, iron-sulfur protein subunit (AAC77113.1); Blastp hit to AAC77113.1 (244 aa), 95% identity in aa 1 - 244; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (244 aa)
yidCPutative preprotein translocase subunit YidC; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. (548 aa)
yhbGPutative ABC superfamily transport protein; Atp_bind; similar to E. coli putative ATP-binding component of a transport system (AAC76233.1); Blastp hit to AAC76233.1 (241 aa), 98% identity in aa 1 - 241. (241 aa)
secGPreprotein translocase IISP family protein; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. (110 aa)
dnaKChaperone Hsp70; Acts as a chaperone. (638 aa)
murGUndecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. (355 aa)
glnDUridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. (890 aa)
proSProline tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves de [...] (572 aa)
STM0353Similar to E. coli putative ATPase (AAC73586.1); Blastp hit to AAC73586.1 (834 aa), 42% identity in aa 99 - 831, 45% identity in aa 4 - 63. (762 aa)
flgBFlagellar biosynthesis protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (138 aa)
flgCFlagellar biosynthesis protein; Cell-proximal portion of basal-body rod; flagellar basal-body rod protein FLGC (putative proximal rod protein). (SW:FLGC_SALTY); Belongs to the flagella basal body rod proteins family. (134 aa)
flgKHook-filament junction protein 1; Flagellar biosynthesis protein; flagellar hook-associated protein 1 (HAP1). (SW:FLGK_SALTY); Belongs to the flagella basal body rod proteins family. (553 aa)
flgLHook-filament junction protein; Flagellar biosynthesis protein; flagellar hook-associated protein 3 (HAP3) (hook-filament junctionprotein). (SW:FLGL_SALTY). (317 aa)
pheTPhenylalanine tRNA synthetase, beta-subunit; phenylalanyl-tRNA synthetase beta chain. (SW:SYFB_SALTY); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 aa)
galUSimilar to E. coli glucose-1-phosphate uridylyltransferase (AAC74318.1); Blastp hit to AAC74318.1 (302 aa), 97% identity in aa 1 - 302. (302 aa)
argSarginyl-tRNA synthetase. (SW:SYR_SALTY). (577 aa)
motBEnables flagellar motor rotation; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). (309 aa)
fliASigma F (sigma 28) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. May regulate the expression of genes involved in virulence. (239 aa)
fliCFlagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (495 aa)
fliHFlagellar biosynthesis protein; Needed for flagellar regrowth and assembly. (235 aa)
fliKFlagellar hook-length control protein; Controls the length of the flagellar hook. (405 aa)
fliMFlagellar biosynthesis protein; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). (334 aa)
nuoNNADH dehydrogenase I chain 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. (425 aa)
nuoMSimilar to E. coli NADH dehydrogenase I chain M (AAC75337.1); Blastp hit to AAC75337.1 (509 aa), 96% identity in aa 1 - 509. (509 aa)
nuoKNADH dehydrogenase I chain 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. (100 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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