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SYP_CAUVN
ID   SYP_CAUVN               Reviewed;         443 AA.
AC   B8GWT1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=CCNA_02008;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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}.
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DR   EMBL; CP001340; ACL95473.1; -; Genomic_DNA.
DR   RefSeq; WP_010919797.1; NC_011916.1.
DR   RefSeq; YP_002517381.1; NC_011916.1.
DR   AlphaFoldDB; B8GWT1; -.
DR   SMR; B8GWT1; -.
DR   PRIDE; B8GWT1; -.
DR   EnsemblBacteria; ACL95473; ACL95473; CCNA_02008.
DR   GeneID; 7333336; -.
DR   KEGG; ccs:CCNA_02008; -.
DR   PATRIC; fig|565050.3.peg.1967; -.
DR   HOGENOM; CLU_016739_4_2_5; -.
DR   OMA; NCDYAAN; -.
DR   OrthoDB; 665824at2; -.
DR   PhylomeDB; B8GWT1; -.
DR   Proteomes; UP000001364; Chromosome.
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; Reference proteome.
FT   CHAIN           1..443
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000185524"
SQ   SEQUENCE   443 AA;  49173 MW;  C9E4FEF540AF7A24 CRC64;
     MRSSRYFLPV LKEAPSDAQI VSHQLMLRAG MIRQEAAGIY AWLPLGLRVL NKIEQIVREE
     MDRAGAIELL MPTIQLADLW RESGRYDDYG DEMLRITDRH KRELLFGPTA EEVVTDIFRA
     SIKSYKDLPK NLYNIQWKFR DERRPRFGVM RGREFLMKDA YSFDLDADGA RKSYNRMFVA
     YLNLFARMGL KAVPMRADTG PIGGDLSHEF IVLAETGESA VFCHKDLVEM PAPGPDLDWI
     NGDLQPLVNQ RTALYAATEE MHDEAAFNAL PEGDRLSARG IEVGHIFSFG TKYSEPMKAT
     VQGPDGQQVP VQMGSYGVGV SRLLGAIIEA SHDEGGIIWP ESVAPFDVGI VNMRQGDAAC
     DAACETAYNA LKAAGREVLY DDTDARGGAK FATMDLIGLP WQLIVGPKGI AEGVVEIKHR
     KTGERHTASL ESVLDGLTKS KTT
 
 
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