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ECOLI:SYP

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) proS (synonyms: drpA)
Protein Name(s) Proline--tRNA ligase

Global RNA synthesis factor Prolyl-tRNA synthetase ProRS

External Links
UniProt P16659
EMBL X55518
M97858
M32357
U70214
U00096
AP009048
D15061
PIR B64744
RefSeq NP_414736.1
YP_488497.1
ProteinModelPortal P16659
SMR P16659
DIP DIP-10573N
IntAct P16659
MINT MINT-1261583
STRING 511145.b0194
SWISS-2DPAGE P16659
PaxDb P16659
PRIDE P16659
EnsemblBacteria AAC73305
BAA77870
GeneID 12932635
949116
KEGG ecj:Y75_p0191
eco:b0194
PATRIC 32115501
EchoBASE EB0763
EcoGene EG10770
eggNOG COG0442
HOGENOM HOG000076893
InParanoid P16659
KO K01881
OMA IQPAELW
OrthoDB EOG6TTVMR
PhylomeDB P16659
BioCyc EcoCyc:PROS-MONOMER
ECOL316407:JW0190-MONOMER
MetaCyc:PROS-MONOMER
SABIO-RK P16659
PRO PR:P16659
Proteomes UP000000318
UP000000625
Genevestigator P16659
GO GO:0005829
GO:0043906
GO:0005524
GO:0004827
GO:0006433
GO:0006450
Gene3D 3.40.50.800
3.90.960.10
HAMAP MF_01569
InterPro IPR002314
IPR006195
IPR004154
IPR002316
IPR004500
IPR023717
IPR007214
PANTHER PTHR11451:SF3
Pfam PF03129
PF00587
PF04073
PRINTS PR01046
SUPFAM SSF52954
SSF55826
TIGRFAMs TIGR00409
PROSITE PS50862

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0043906

Ala-tRNA(Pro) hydrolase activity

PMID:14530268[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006433

prolyl-tRNA aminoacylation

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10770
PANTHER:PTN000154976

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10770
PANTHER:PTN000155068

C

Seeded From UniProt

complete

enables

GO:0004827

proline-tRNA ligase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10770
PANTHER:PTN000154976

F

Seeded From UniProt

complete

involved_in

GO:0006433

prolyl-tRNA aminoacylation

PMID:6991867[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004827

proline-tRNA ligase activity

PMID:9062123[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0106074

aminoacyl-tRNA metabolism involved in translational fidelity

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0002161

P

Seeded From UniProt

complete

involved_in

GO:0106074

aminoacyl-tRNA metabolism involved in translational fidelity

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0043906

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002314

F

Seeded From UniProt

complete

enables

GO:0002161

aminoacyl-tRNA editing activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007214
InterPro:IPR036754

F

Seeded From UniProt

complete

enables

GO:0004812

aminoacyl-tRNA ligase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002314

F

Seeded From UniProt

complete

enables

GO:0004827

proline-tRNA ligase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002316
InterPro:IPR004500
InterPro:IPR023717

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002314
InterPro:IPR002316
InterPro:IPR004500
InterPro:IPR023717

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002316
InterPro:IPR004500
InterPro:IPR023717

C

Seeded From UniProt

complete

involved_in

GO:0006418

tRNA aminoacylation for protein translation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002314

P

Seeded From UniProt

complete

involved_in

GO:0006433

prolyl-tRNA aminoacylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002316
InterPro:IPR004500
InterPro:IPR023717

P

Seeded From UniProt

complete

enables

GO:0004827

proline-tRNA ligase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:6.1.1.15

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000038401

F

Seeded From UniProt

complete

enables

GO:0004827

proline-tRNA ligase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000038401

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000038401

C

Seeded From UniProt

complete

involved_in

GO:0006433

prolyl-tRNA aminoacylation

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000038401

P

Seeded From UniProt

complete

enables

GO:0004812

aminoacyl-tRNA ligase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0030

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0006412

translation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0648

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0016874

ligase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0436

F

Seeded From UniProt

complete

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Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Wong, FC et al. (2003) An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing. J. Biol. Chem. 278 52857-64 PubMed GONUTS page
  2. ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Bohman, K & Isaksson, LA (1980) A temperature-sensitive mutant in prolinyl-tRNA ligase of Escherichia coli K-12. Mol. Gen. Genet. 177 603-5 PubMed GONUTS page
  5. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  6. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  7. ↑ Stehlin, C et al. (1997) Chemical modification and site-directed mutagenesis of the single cysteine in motif 3 of class II Escherichia coli prolyl-tRNA synthetase. Biochemistry 36 2932-8 PubMed GONUTS page
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