ID   SYP_PSEA7               Reviewed;         571 AA.
AC   A6VA16;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569};
DE            Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569};
GN   Name=proS {ECO:0000255|HAMAP-Rule:MF_01569}; OrderedLocusNames=PSPA7_4552;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-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). As ProRS can
CC       inadvertently accommodate and process non-cognate amino acids such as
CC       alanine and cysteine, to avoid such errors it has two additional
CC       distinct editing activities against alanine. One activity is designated
CC       as 'pretransfer' editing and involves the tRNA(Pro)-independent
CC       hydrolysis of activated Ala-AMP. The other activity is designated
CC       'posttransfer' editing and involves deacylation of mischarged Ala-
CC       tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
CC       {ECO:0000255|HAMAP-Rule:MF_01569}.
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_01569};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       editing domain and the C-terminal anticodon-binding domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}.
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; CP000744; ABR81676.1; -; Genomic_DNA.
DR   RefSeq; WP_003155969.1; NC_009656.1.
DR   AlphaFoldDB; A6VA16; -.
DR   SMR; A6VA16; -.
DR   PRIDE; A6VA16; -.
DR   EnsemblBacteria; ABR81676; ABR81676; PSPA7_4552.
DR   KEGG; pap:PSPA7_4552; -.
DR   HOGENOM; CLU_016739_0_0_6; -.
DR   OMA; NCDYAAN; -.
DR   OrthoDB; 665824at2; -.
DR   Proteomes; UP000001582; 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; cd00861; ProRS_anticodon_short; 1.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.30.930.10; -; 2.
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; 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; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR   InterPro; IPR044140; ProRS_anticodon_short.
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; SSF55681; SSF55681; 1.
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;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..571
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000069154"
SQ   SEQUENCE   571 AA;  63057 MW;  4AF8A694DDB7B84F CRC64;
     MRTSQYLLST LKETPADAVV ISHQLLLRAG MIRRLASGLY TWLPMGLRVL RKVETVVREE
     MNAAGALEVL MPAVQPAELW QESGRWEQYG PELLRLKDRH EREFCVGPTH EEVITDLARN
     ELNSYKQLPI NFYQIQTKFR DEIRPRFGLM RGREFIMKDA YSFHLNQESL QATYDGMYQA
     YSKIFTRLGL DFRPVQADNG SIGGSGSHEF HVLANSGEDD IVFSDSSDYA ANIEKAEAVP
     RESARGAASE DMRLVDTPDT KTIAALVDGF GLPIEKTIKT LVVHGAEEGT LVALIVRGDH
     ELNEIKAANQ PLVASPLVFA SEAEIRAAIG AGPGSLGPVN LPIACIVDRS VALMSDFAAG
     ANIEDKHYFG VNWERDLPLP EVADLRNVVE GDPSPDGKGT LVIKRGIEVG HIFQLGTKYS
     EAMKLSVLSE QGKPVNLIMG CYGIGVSRVV AAAIEQNHDE RGILWPSALA PFQIALVPLK
     YETESVRQAT DRLYAELTAA GFEVLLDDRD KKTSPGVKFA DMELLGIPHR IVVSDRGLNE
     GVLEYKGRRD SESQNLPIGE LMSFITEKLS R