ID SYP_STRSV Reviewed; 616 AA.
AC A3CQI5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 01-MAY-2013, entry version 48.
DE RecName: Full=Proline--tRNA ligase;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
GN Name=proS; OrderedLocusNames=SSA_2069;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S.,
RA Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y.,
RA Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L.,
RA Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
CC diphosphate + L-prolyl-tRNA(Pro).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic
CC domain, the editing domain and the C-terminal anticodon-binding
CC domain (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. ProS type 1 subfamily.
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DR EMBL; CP000387; ABN45440.1; -; Genomic_DNA.
DR RefSeq; YP_001035990.1; NC_009009.1.
DR ProteinModelPortal; A3CQI5; -.
DR SMR; A3CQI5; 1-614.
DR STRING; 388919.SSA_2069; -.
DR EnsemblBacteria; ABN45440; ABN45440; SSA_2069.
DR GeneID; 4806247; -.
DR KEGG; ssa:SSA_2069; -.
DR PATRIC; 19771055; VBIStrSan33173_1962.
DR eggNOG; COG0442; -.
DR HOGENOM; HOG000076893; -.
DR KO; K01881; -.
DR OMA; IQPAELW; -.
DR ProtClustDB; PRK09194; -.
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:HAMAP.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:HAMAP.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:GOC.
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_cons-dom.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004154; Anticodon-bd.
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; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR PANTHER; PTHR11451:SF3; PTHR11451:SF3; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF04073; YbaK; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF52954; Anticodon_bd; 1.
DR SUPFAM; SSF55826; YbaK/aa-tRNA-synth-assoc-reg; 1.
DR TIGRFAMs; TIGR00409; proS_fam_II; 2.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1 616 Proline--tRNA ligase.
FT /FTId=PRO_0000288383.
SQ SEQUENCE 616 AA; 68571 MW; 211961C324AC567F CRC64;
MKQSKMLIPT LREMPSDAQV ISHALMLRAG YVRQVSAGVY SYLPLANRVI EKAKRIMREE
FDKIGAVEML APALLSADLW RESGRYETYG EDLYKLKNRE KSDFILGPTH EETFTAIVRD
SVKSYKQLPL NLYQIQPKYR DEKRPRNGLL RTREFIMKDA YSFHANYDSL DVAYDEYKSA
YEKIFTRSEL DFKAIIGDGG AMGGKDSQEF MAITPDRTDL NRWVVLDKSV ASFDEIPEDV
QEAIRTELTS WMVSGEDTIA YSSESSYAAN LEMATDEYKP AGRVVTEEEV ARVSTPDCKT
IDEVAAFLGL DESQTIKTLV YMADESPVVA LLVGNDQLNE VKLKNHLAAD FFDVASEDQV
RQLLGAGFGS LGPVNLPEGV RIIADRKVQD LANAVVGANE DGYHLTGVNP GRDFTAEFVD
IREVREGEIS PDGQGVLKFA RGIEIGHIFK LGTRYSDSMN ANVLDENGRA VPMIMGCYGI
GVSRLLSAVM EQHARLFVNK TPKGEFRYAW GINFPKELAP FDVHLIPVNV KDEEALALTD
QIEANLLSAG YEVLVDDRNE RAGVKFSDSD LIGLPIRVTV GKKAAEGIVE VKIKATGDTI
EVHADNLLET LSILTK
//
