STRINGSTRING
infB infB prfB prfB lysS lysS alaS alaS lepA lepA hisS hisS gltX gltX metG metG argS argS aspS aspS infC infC pheS pheS pheT pheT tyrS tyrS yciH yciH prfA prfA leuS leuS cysS cysS ybaK ybaK proS proS asnS asnS frr frr tsf tsf ileS ileS thrS thrS yeaK yeaK serS serS infA infA rimK rimK glnS glnS prfC prfC STM4549 STM4549 trpS2 trpS2 valS valS efp efp selA selA glyQ glyQ glyS glyS trpS trpS fusA fusA tufA tufA fmt fmt def def
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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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infBProtein chain initiation factor IF-2; One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity). (892 aa)
prfBPeptide chain release factor RF-2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. (293 aa)
lysSSimilar to E. coli lysine tRNA synthetase, constitutive; suppressor of ColE1 mutation in primer RNA (AAC75928.1); Blastp hit to AAC75928.1 (505 aa), 95% identity in aa 1 - 505; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 aa)
alaSalanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family. (876 aa)
lepAGTP-binding elongation factor; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. (599 aa)
hisShistidyl-tRNA synthetase. (SW:SYH_SALTY). (424 aa)
gltXGlutamate tRNA synthetase, catalytic subunit; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (471 aa)
metGMethionine tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (677 aa)
argSarginyl-tRNA synthetase. (SW:SYR_SALTY). (577 aa)
aspSAspartate tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (590 aa)
infCProtein chain initiation factor IF-3; IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. (144 aa)
pheSSimilar to E. coli phenylalanine tRNA synthetase, alpha-subunit (AAC74784.1); Blastp hit to AAC74784.1 (327 aa), 97% identity in aa 1 - 327. (327 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)
tyrSTyrosine tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. (424 aa)
yciHPutative translation initiation factor SUI1; Protein YCIH. (SW:YCIH_SALTY); Belongs to the SUI1 family. (108 aa)
prfAPeptide chain release factor RF-1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. (360 aa)
leuSSimilar to E. coli leucine tRNA synthetase (AAC73743.1); Blastp hit to AAC73743.1 (860 aa), 95% identity in aa 1 - 860; Belongs to the class-I aminoacyl-tRNA synthetase family. (860 aa)
cysSSimilar to E. coli cysteine tRNA synthetase (AAC73628.1); Blastp hit to AAC73628.1 (461 aa), 94% identity in aa 1 - 461; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
ybaKPutative cytoplasmic protein; Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity. (159 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)
asnSSimilar to E. coli asparagine tRNA synthetase (AAC74016.1); Blastp hit to AAC74016.1 (466 aa), 94% identity in aa 1 - 466. (466 aa)
frrRibosome releasing factor; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another; Belongs to the RRF family. (185 aa)
tsfProtein chain elongation factor EF-Ts; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family. (283 aa)
ileSIsoleucine tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. (944 aa)
thrSThreonine tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). (642 aa)
yeaKPutative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC74857.1); Blastp hit to AAC74857.1 (167 aa), 87% identity in aa 1 - 165. (172 aa)
serSSerine tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (430 aa)
infAProtein chain initiation factor IF-1; One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. (72 aa)
rimKRibosomal protein S6 modification protein; Is an L-glutamate ligase that catalyzes the ATP-dependent post-translational addition of glutamate residues to the C-terminus of ribosomal protein S6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH. Belongs to the RimK family. (300 aa)
glnSSimilar to E. coli glutamine tRNA synthetase (AAC73774.1); Blastp hit to AAC73774.1 (554 aa), 96% identity in aa 1 - 554. (555 aa)
prfCPeptide chain release factor RF-3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily. (529 aa)
STM4549Putative cytoplasmic protein. (152 aa)
trpS2Putative tryptophanyl-tRNA synthetase; Similar to E. coli tryptophan tRNA synthetase (AAC76409.1); Blastp hit to AAC76409.1 (334 aa), 26% identity in aa 2 - 329; Belongs to the class-I aminoacyl-tRNA synthetase family. (337 aa)
valSValine tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (951 aa)
efpElongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation. (188 aa)
selASelenocysteine synthase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis; Belongs to the SelA family. (463 aa)
glyQSimilar to E. coli glycine tRNA synthetase, alpha subunit (AAC76584.1); Blastp hit to AAC76584.1 (303 aa), 99% identity in aa 1 - 303. (303 aa)
glySSimilar to E. coli glycine tRNA synthetase, beta subunit (AAC76583.1); Blastp hit to AAC76583.1 (689 aa), 92% identity in aa 1 - 689. (689 aa)
trpSTryptophan tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
fusAProtein chain elongation factor EF-G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPas [...] (704 aa)
tufAProtein chain elongation factor EF-Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (394 aa)
fmt10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. (315 aa)
defPeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. (169 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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