SYP_BRUC2
ID SYP_BRUC2 Reviewed; 442 AA.
AC A9MAJ9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01570};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01570};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01570};
DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01570};
GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01570}; OrderedLocusNames=BCAN_A0837;
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-
CC step reaction: proline is first activated by ATP to form Pro-AMP and
CC then transferred to the acceptor end of tRNA(Pro). {ECO:0000255|HAMAP-
CC Rule:MF_01570}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC EC=6.1.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01570};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01570}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01570}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000872; ABX61902.1; -; Genomic_DNA.
DR RefSeq; WP_004690762.1; NC_010103.1.
DR AlphaFoldDB; A9MAJ9; -.
DR SMR; A9MAJ9; -.
DR EnsemblBacteria; ABX61902; ABX61902; BCAN_A0837.
DR GeneID; 55590532; -.
DR KEGG; bcs:BCAN_A0837; -.
DR HOGENOM; CLU_016739_4_2_5; -.
DR OMA; NCDYAAN; -.
DR PhylomeDB; A9MAJ9; -.
DR Proteomes; UP000001385; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_01570; Pro_tRNA_synth_type2; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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; IPR023716; Prolyl-tRNA_ligase_IIa_type2.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..442
FT /note="Proline--tRNA ligase"
FT /id="PRO_1000087861"
SQ SEQUENCE 442 AA; 49508 MW; D7A2C65987954862 CRC64;
MRLSRYFLPI LKENPKEAEI VSHRLMLRSG MIRQQSAGIY SWLPIGLKVL NKVCTIIREE
QNRAGANEIL MPTIQSADLW RESGRYDAYG KEMLRIQDRQ EREMLFGPTN EEMVTDIFRS
YVRSYKDLPL NLYHIQWKFR DEVRPRFGVM RSREFLMKDA YSFDLDYEGA KMAYYRMFVS
YLRTFARVGL QAIPMRADTG PIGGDLSHEF IILAETGESQ VYCDRAYLDL AVPGADTDFR
NDAQLTDIVT RWTTPYAATD EMHDEADWAK VKPESQVSAR GIEVGHIFHF GTKYSEPMGA
KVQGPDGKEH LVSMGSYGIG PSRLVAAAIE ASHDDAGIIW PKAIAPFGAG IVNMKPGDEG
CDGVSEKLYE ALTNAGVDPL LDDKDERPGA KFATMDLIGL PTQVIVGPRG VAAGEVEVKD
RKMGERQSLG IEAAINMLTA QA