ID   SYP_PSYWF               Reviewed;         576 AA.
AC   A5WDG2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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};
GN   OrderedLocusNames=PsycPRwf_0751;
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=349106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP000713; ABQ93703.1; -; Genomic_DNA.
DR   RefSeq; WP_011960026.1; NC_009524.1.
DR   AlphaFoldDB; A5WDG2; -.
DR   SMR; A5WDG2; -.
DR   STRING; 349106.PsycPRwf_0751; -.
DR   EnsemblBacteria; ABQ93703; ABQ93703; PsycPRwf_0751.
DR   KEGG; prw:PsycPRwf_0751; -.
DR   eggNOG; COG0442; Bacteria.
DR   HOGENOM; CLU_016739_0_0_6; -.
DR   OMA; NCDYAAN; -.
DR   OrthoDB; 665824at2; -.
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   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..576
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000073591"
SQ   SEQUENCE   576 AA;  64128 MW;  8F84A32567449D04 CRC64;
     MRASQFLFAT LKETPSDADI VSSQLMLRAG LIRKLASGLY VWLPMGLKVL QKVEKIVREE
     MQNIGGQEVL MPMTQPAELW QESGRFEDYG PELLRFTDRH NRDFVLGPTH EEVITDLARG
     ELRSYKQLPV TFFQIQGKFR DEIRPRFGIM RAREFTMKDA YSFHVDQASL EVTYQQMYDA
     YTRIFQRLGL NFRAVLADTG SIGGSASHEF HVLAGSGEDA IAFSDGSDYA ANVELAEAIC
     TDERAAPTQD KQNVSTPKIQ TNEELAKFLD IPLHTTVKTL VVKGHRINED GSEGDEQLVA
     LVVRGDHTLN EIKAEKIAEV ATPLTFATEE EMKAAGLKKG FIGVDLDMPV YVDRAAAALS
     DFVSGANEYD MHTTGMNWER DATITDVVDI RNVVEGDASP DGKGTLSIKR GIEVGHIFQL
     GDKYSKALNC TVMGEDGKPV TLMMGCYGIG VSRIIAAAIE QNHDDNGIIW AKTPDIKDSI
     APFDIAIVPM KSKEDTVMQT AEALYEELKA RGLNVILDDR NERPGVKFAD LELIGIPHRI
     VVSDRNLAED KYEYVDRRDG EKQLLSREEL LAKVSL