ID   SYP_FRATM               Reviewed;         565 AA.
AC   B2SFQ6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=FTM_0608;
OS   Francisella tularensis subsp. mediasiatica (strain FSC147).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=441952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC147;
RX   PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA   Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA   Keim P., Johansson A.;
RT   "Molecular evolutionary consequences of niche restriction in Francisella
RT   tularensis, a facultative intracellular pathogen.";
RL   PLoS Pathog. 5:E1000472-E1000472(2009).
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; CP000915; ACD30599.1; -; Genomic_DNA.
DR   RefSeq; WP_012429334.1; NC_010677.1.
DR   AlphaFoldDB; B2SFQ6; -.
DR   SMR; B2SFQ6; -.
DR   KEGG; ftm:FTM_0608; -.
DR   HOGENOM; CLU_016739_0_0_6; -.
DR   OMA; NCDYAAN; -.
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   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..565
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000199388"
SQ   SEQUENCE   565 AA;  63617 MW;  D1C6CE88849AB3D0 CRC64;
     MKATQTLIAT TKELPKEAVL ISHQYMLKAG LIKKLASGIY TWMPLGLKVL QKIQNIVRDE
     MNKAGASELL LPSILPSELL QETHRWDKFG PELLKLHDRH NRDFCYGPTH EEPIVDMARD
     TIKSYKQLPL NLYQIQTKFR DEIRPRFGVM RAREFIMKDA YSFHENSQCL RNTYNTMYAT
     YCNILDKIGL AYRPVKADTG AIGGDNSHEF QVLANAGEDI ICYSNGSDYA ANIELATYAK
     PDLSKRVNSQ NTIEKIHTPN IKTIEKLYKE MSFDIKKTIK TMVIKDAGGN FFALVIRGDH
     ELNETKINKL DQIIAPYTLA TKEEIFSIFN ANPGSLGIYN CPISIIADYS AIAITDLVCG
     ANEDDYHFTN VNWDRDVTNY QIADIRNVVT GDISPDCKGT LELTNGIEVG HIFELEDVYS
     KPMNANIIGQ DGKSKPMLMG CYGFGVSRVM AAAIEQSHDE NGIIWPESIA PYQVAILPIN
     YNKSDKVKEV ADKLYQDLLG DGIDVLLDDR GARPGVMFAD ADLIGYSHHV VIGDKLLEQG
     LIEYKNRKTQ EKQEITIAEL IKILK