(data stored in ACNUC10821 zone)

SWISSPROT: C8U1R2_ECO10

ID   C8U1R2_ECO10            Unreviewed;       572 AA.
AC   C8U1R2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01569};
DE            EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01569};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01569};
DE            Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01569};
GN   Name=proS {ECO:0000256|HAMAP-Rule:MF_01569,
GN   ECO:0000313|EMBL:BAI29070.1};
GN   OrderedLocusNames=ECO103_0194 {ECO:0000313|EMBL:BAI29070.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29070.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29070.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a
CC       two-step reaction: proline is first activated by ATP to form Pro-
CC       AMP and then transferred to the acceptor end of tRNA(Pro). As
CC       ProRS can inadvertently accommodate and process non-cognate amino
CC       acids such as alanine and cysteine, to avoid such errors it has
CC       two additional distinct editing activities against alanine. One
CC       activity is designated as 'pretransfer' editing and involves the
CC       tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other
CC       activity is designated 'posttransfer' editing and involves
CC       deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-
CC       tRNA(Pro) is not edited by ProRS. {ECO:0000256|HAMAP-
CC       Rule:MF_01569, ECO:0000256|SAAS:SAAS00761654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-
CC         prolyl-tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700,
CC         Rhea:RHEA-COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:60039, ChEBI:CHEBI:78442, ChEBI:CHEBI:78532,
CC         ChEBI:CHEBI:456215; EC=6.1.1.15; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01569, ECO:0000256|SAAS:SAAS01124670};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01569,
CC       ECO:0000256|SAAS:SAAS00632876}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01569,
CC       ECO:0000256|SAAS:SAAS00632870}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic
CC       domain, the editing domain and the C-terminal anticodon-binding
CC       domain. {ECO:0000256|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01569,
CC       ECO:0000256|SAAS:SAAS00632846}.
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DR   EMBL; AP010958; BAI29070.1; -; Genomic_DNA.
DR   RefSeq; WP_001260712.1; NC_013353.1.
DR   SMR; C8U1R2; -.
DR   EnsemblBacteria; BAI29070; BAI29070; ECO103_0194.
DR   KEGG; eoh:ECO103_0194; -.
DR   HOGENOM; HOG000076893; -.
DR   KO; K01881; -.
DR   OMA; QESGRWD; -.
DR   BioCyc; ECOL585395:ECO103_RS00990-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   Gene3D; 3.90.960.10; -; 1.
DR   HAMAP; MF_01569; Pro_tRNA_synth_type1; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR   InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR   InterPro; IPR033730; ProRS_core_prok.
DR   InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF04073; tRNA_edit; 1.
DR   PIRSF; PIRSF001535; ProRS_1; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF55826; SSF55826; 1.
DR   TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1R2.
DR   SWISS-2DPAGE; C8U1R2.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682373, ECO:0000313|EMBL:BAI29070.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682365};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00632883};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682366};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682360};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682364}.
FT   DOMAIN       38    468       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   572 AA;  63623 MW;  1E5E482D53A28AFD CRC64;
     MRTSQYLLST LKETPADAEV ISHQLMLRAG MIRKLASGLY TWLPTGVRVL KKVENIVREE
     MNNAGAIEVS MPVVQPADLW QESGRWEQYG PELLRFVDRG ERPFVLGPTH EEVITDLIRN
     ELSSYKQLPL NFYQIQTKFR DEVRPRFGVM RSREFLMKDA YSFHTSQESL QETYDAMYAA
     YSKIFSRMGL DFRAVQADTG SIGGSASHEF QVLAQSGEDD VVFSDTSDYA ANIELAEAIA
     PKEPRAAATQ EMTLVDTPNA KTIAELVEQF NLPIEKTVKT LLVKAVEGSS FPLVALLVRG
     DHELNEVKAE KLPQVASPLT FATEEEIRAV VKAGPGSLGP VNMPIPVVID RTVAAMSDFA
     AGANIDGKHY FGINWDRDVA TPEVADIRNV VAGDPSPDGQ GTLLIKRGIE VGHIFQLGTK
     YSEALKASVQ GEDGRNQILT MGCYGIGVTR VVAAAIEQNY DERGIVWPDA IAPFQVAILP
     MNMHKSFRVQ ELAEKLYSEL RAQGIEVLLD DRKERPGVMF ADMELIGIPH TIVLGDRNLD
     NDDIEYKYRR NGEKQLIKTG DIVEYLVKQI KG
//

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