ID   SYP_RICCN               Reviewed;         426 AA.
AC   Q92I92;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01570};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01570};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01570};
DE            Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01570};
GN   Name=proS {ECO:0000255|HAMAP-Rule:MF_01570}; OrderedLocusNames=RC0528;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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). {ECO:0000255|HAMAP-
CC       Rule:MF_01570}.
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_01570};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01570}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01570}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01570}.
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DR   EMBL; AE006914; AAL03066.1; -; Genomic_DNA.
DR   PIR; H97765; H97765.
DR   RefSeq; WP_010977166.1; NC_003103.1.
DR   AlphaFoldDB; Q92I92; -.
DR   SMR; Q92I92; -.
DR   EnsemblBacteria; AAL03066; AAL03066; RC0528.
DR   KEGG; rco:RC0528; -.
DR   PATRIC; fig|272944.4.peg.604; -.
DR   HOGENOM; CLU_016739_4_2_5; -.
DR   OMA; NCDYAAN; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_01570; Pro_tRNA_synth_type2; 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; IPR023716; Prolyl-tRNA_ligase_IIa_type2.
DR   InterPro; IPR044140; ProRS_anticodon_short.
DR   InterPro; IPR033730; ProRS_core_prok.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF55681; SSF55681; 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..426
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000248915"
SQ   SEQUENCE   426 AA;  48472 MW;  F9393F3CB7A261B6 CRC64;
     MLLSKYFLPV LKEEPSEAQV TSHKLMLRSG MIRQQAAGIY TWLPLGLKVL KNIENIVRLN
     MNKAGALEVL MPCIQPAHLW MESGRFDNYG KEMLKFQDRH DNTLLFGPTN EDMITDIFRH
     NIKSYKDLPK NLYHIQWKFR DEIRPRFGVM RGREFLMKDA YSFDINEENA VKTYNQMYKA
     YINAFRDLGV FVIPVIADNG PIGGNLSHEF HIIAETGEST IYYDKKFKTL KDNPDIDVEE
     IKSWYAAAEE KYEVNKLPIS EQEITSSKGI EVGHIFYIGS KYSVNMNALI NDEYGKLTPI
     EMSSYGIGIS RLVAAIIEAN CDEKGIIWPS SVAPFKVSLI NLNIHDSKCV ELAEMAYKEL
     SDKNIEVLYD DTEARPGSKF ATHDLIGSPH QIIIGPKKAA NNIVELKDRK SGVIEDIEVG
     SLMSVL