ID SYP_PSEA8 Reviewed; 571 AA.
AC B7UXX6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 33.
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=PLES_43581;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L.,
RA Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D.,
RA Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L.,
RA Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants
RT of in vivo competitiveness in the Liverpool epidemic strain of
RT Pseudomonas aeruginosa.";
RL Genome Res. 19:12-23(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 (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; FM209186; CAW29113.1; -; Genomic_DNA.
DR RefSeq; YP_002441942.1; NC_011770.1.
DR ProteinModelPortal; B7UXX6; -.
DR SMR; B7UXX6; 1-221.
DR STRING; 557722.PLES_43581; -.
DR EnsemblBacteria; CAW29113; CAW29113; PLES_43581.
DR GeneID; 7178410; -.
DR KEGG; pag:PLES_43581; -.
DR PATRIC; 19818532; VBIPseAer113719_4489.
DR eggNOG; COG0442; -.
DR HOGENOM; HOG000076893; -.
DR KO; K01881; -.
DR OMA; IQPAELW; -.
DR ProtClustDB; PRK09194; -.
DR BioCyc; PAER557722:GHJW-5590-MONOMER; -.
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; 1.
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 1 571 Proline--tRNA ligase.
FT /FTId=PRO_1000199411.
SQ SEQUENCE 571 AA; 63104 MW; 2380758D2523CD14 CRC64;
MRTSQYLLST LKETPADAVV ISHQLLLRAG MIRRLASGLY TWLPMGLRVL RKVETIVREE
MNAAGALEVL MPAVQPAELW QESGRWEQYG PELLRLKDRH EREFCVGPTH EEVITDLARN
ELNSYKQLPI NFYQIQTKFR DEIRPRFGLM RGREFIMKDA YSFHLSQDSL QQTYDGMYQA
YSKIFSRLGL DFRPVQADNG SIGGSGSHEF HVLANSGEDD IVFSDSSDYA ANIEKAEAVP
RESARGSATE DMRLVDTPNT KTIAALVDGF QLPIEKTIKT LVVHGAEEGT LVALIVRGDH
ELNEIKAANQ PLVASPLVFA SEAEIRAAIG AGPGSLGPVN LPIACIVDRS VALMSDFAAG
ANIEDKHYFG VNWERDLPLP EVADLRNVVE GDPSPDGKGT LVIKRGIEVG HIFQLGTKYS
EAMKLSVLSE QGKPVNLIMG CYGIGVSRVV AAAIEQNHDE RGILWPSALA PFQIALVPLK
YETESVKQAT DKLYAELTAA GFEVLLDDRD KKTSPGVKFA DMELIGIPHR IVISDRGLSE
GVLEYKGRRD SESQNLPIGE LMSFITEKLS R
//
