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nuoK nuoK nuoL nuoL lexA lexA hemD hemD atpG atpG atpC atpC dnaA dnaA pitA pitA recA recA nadB nadB htrA htrA sdhC sdhC sdhA sdhA cydA cydA cydB cydB galE galE nlpC nlpC slp slp yeaZ yeaZ cbiA cbiA nuoN nuoN nuoC nuoC murQ murQ nuoE nuoE nuoG nuoG nuoH nuoH nuoI nuoI nuoJ nuoJ
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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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)
nuoLSimilar to E. coli NADH dehydrogenase I chain L (AAC75338.1); Blastp hit to AAC75338.1 (613 aa), 94% identity in aa 1 - 613. (613 aa)
lexASOS response regulator; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single- stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. (202 aa)
hemDUroporphyrinogen III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. Belongs to the uroporphyrinogen-III synthase family. (246 aa)
atpGMembrane-bound ATP 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. (287 aa)
atpCMembrane-bound ATP synthase, F1 sector, epsilon-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (139 aa)
dnaADNA replication initiator protein; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. DnaA can inhibit its own gene expression as well as that of other genes (By similarity). (466 aa)
pitAPiT family; similar to E. coli low-affinity phosphate transport (AAC76518.1); Blastp hit to AAC76518.1 (499 aa), 92% identity in aa 1 - 499. (498 aa)
recADNA strand exchange and recombination protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. (353 aa)
nadBQuinolinate synthetase, B protein; Catalyzes the oxidation of L-aspartate to iminoaspartate. (540 aa)
htrAPeriplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] (475 aa)
sdhCSuccinate dehydrogenase, cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (129 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa)
cydASimilar to E. coli cytochrome d terminal oxidase, polypeptide subunit I (AAC73827.1); Blastp hit to AAC73827.1 (523 aa), 96% identity in aa 2 - 523. (522 aa)
cydBSimilar to E. coli cytochrome d terminal oxidase polypeptide subunit II (AAC73828.1); Blastp hit to AAC73828.1 (379 aa), 92% identity in aa 1 - 379. (379 aa)
galEUDP-galactose 4-epimerase; Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD (By similarity). (338 aa)
nlpCLipoprotein; Similar to E. coli lipoprotein (AAC74778.1); Blastp hit to AAC74778.1 (154 aa), 86% identity in aa 1 - 154. (154 aa)
slpSimilar to E. coli putative outer membrane protein (AAC74876.1); Blastp hit to AAC74876.1 (193 aa), 90% identity in aa 1 - 193. (193 aa)
yeaZPutative molecular chaperone; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity). Neither binds polyphosphates nor a wide range of nucleotides on its own. Does n [...] (231 aa)
cbiASynthesis of vitamin B12 adenosyl cobalamide precursor; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Is able to use other nucleotide triphosphates as substrate, such as GTP or UTP, although less efficiently than ATP; Belongs to the CobB/CbiA family. (459 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)
nuoCNADH 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. (600 aa)
murQPutative aminotransferase; Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D- lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling; Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily. (297 aa)
nuoENADH dehydrogenase I chain E; 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 (By similarity); Belongs to the complex I 24 kDa subunit family. (166 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. 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 (By similarity). (910 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)
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)
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. (184 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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