STRINGSTRING
panC panC lysS lysS argG argG ileS ileS etfA etfA etfB etfB trmU trmU BARCL_0438 BARCL_0438 trpS trpS ribF ribF cysS cysS coaD coaD argS argS tyrS tyrS ttcA ttcA metS metS gltX gltX nadE nadE gltX-2 gltX-2 valS valS guaA guaA nadD nadD tilS tilS leuS leuS BARCL_1288 BARCL_1288
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:
panCPantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (281 aa)
lysSFragment of peptide chain release factor 3 (part 1); Belongs to the class-I aminoacyl-tRNA synthetase family. (554 aa)
argGArgininosuccinate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (407 aa)
ileSIsoleucyl-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). (971 aa)
etfAElectron transfer flavoprotein alpha-subunit. (309 aa)
etfBElectron transfer flavoprotein beta-subunit. (248 aa)
trmUtRNA(5-methylaminomethyl-2-thiouridylate)- methyltransferase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. (409 aa)
BARCL_0438Homologs of previously reported genes of unknown function. (163 aa)
trpSTryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (355 aa)
ribFRiboflavin biosynthesis protein RibF; Belongs to the ribF family. (330 aa)
cysSCysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (502 aa)
coaDPhosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. (164 aa)
argSArginyl-tRNA synthetase. (588 aa)
tyrSTyrosyl-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. (417 aa)
ttcAConserved protein of unknown function; Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. (272 aa)
metSMethionyl-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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. (513 aa)
gltXglutamyl-tRNA synthetase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (462 aa)
nadENH3-dependent NAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. (558 aa)
gltX-2glutamyl-tRNA synthetase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (476 aa)
valSValyl-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. (907 aa)
guaAGMP synthase; Catalyzes the synthesis of GMP from XMP. (518 aa)
nadDNicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). (208 aa)
tilStRNA(Ile)-lysidine synthase (tRNA(Ile)-lysidine synthetase) (tRNA(Ile)-2-lysyl-cytidine synthase); Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. (481 aa)
leuSLeucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (874 aa)
BARCL_1288Homologs of previously reported genes of unknown function. (225 aa)
Your Current Organism:
Bartonella clarridgeiae
NCBI taxonomy Id: 696125
Other names: B. clarridgeiae 73, Bartonella clarridgeiae 73, Bartonella clarridgeiae str. 73, Bartonella clarridgeiae strain 73
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.