ID   SYP_BORBU               Reviewed;         488 AA.
AC   O51363;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 136.
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=BB_0402;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [2]
RP   PROLINE AND CYSTEINE ACTIVATION, AND KINETIC PARAMETERS.
RX   PubMed=12130657; DOI=10.1074/jbc.m206928200;
RA   Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H.,
RA   Hartsch T., Soell D.;
RT   "Cysteine activation is an inherent in vitro property of prolyl-tRNA
RT   synthetases.";
RL   J. Biol. Chem. 277:34743-34748(2002).
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). Can inadvertently
CC       accommodate and process cysteine.
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;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.17 mM for proline {ECO:0000269|PubMed:12130657};
CC         KM=0.18 mM for cysteine {ECO:0000269|PubMed:12130657};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       anticodon-binding domain and the C-terminal extension. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 3 subfamily. {ECO:0000305}.
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DR   EMBL; AE000783; AAC66767.1; -; Genomic_DNA.
DR   PIR; A70150; A70150.
DR   RefSeq; NP_212536.1; NC_001318.1.
DR   RefSeq; WP_010889744.1; NC_001318.1.
DR   AlphaFoldDB; O51363; -.
DR   SMR; O51363; -.
DR   STRING; 224326.BB_0402; -.
DR   PRIDE; O51363; -.
DR   EnsemblBacteria; AAC66767; AAC66767; BB_0402.
DR   KEGG; bbu:BB_0402; -.
DR   PATRIC; fig|224326.49.peg.796; -.
DR   HOGENOM; CLU_001882_4_2_12; -.
DR   OMA; EVYWVTH; -.
DR   SABIO-RK; O51363; -.
DR   Proteomes; UP000001807; 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; cd00778; ProRS_core_arch_euk; 1.
DR   Gene3D; 3.30.110.30; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR   InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR   InterPro; IPR017449; Pro-tRNA_synth_II.
DR   InterPro; IPR033721; ProRS_core_arch_euk.
DR   PANTHER; PTHR43382; PTHR43382; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   SUPFAM; SSF64586; SSF64586; 1.
DR   TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..488
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000139321"
SQ   SEQUENCE   488 AA;  56311 MW;  96E036EA479FFB60 CRC64;
     MSDFIASKED DYSKWYLDIV QKAKLADYSP VKGCMVIMPY GYSIWSKIQS ILDKKFKETG
     HENAYFPMLI PYSFLEREKD HIDGFSPEFA IIKDAGGESL AEPLVLRPTS ETIIWNMYSK
     WIKSYRDLPL KINQWANVVR WEKRTRPFLR TTEFLWQEGH TAHATEEEAL EETLLILDVY
     KRFIEDYLAI PVFCGKKSEK EKFAGAVSTY SIEALMQDKK ALQAATSHYL GLNFAKAFDV
     KFQDKDGKMR HVFASSWGVS TRLIGALIMV HSDEKGLVLP PRIAPIEIIV IPIFKKEDEI
     NKKILDYSDC VVDALKKAEF RVEIDKDVRS SPGFRFSSAE FKGIPIRLEV GINDVLLNSV
     TISRRDKDRK FKYQISLDSL ISKVKVELDL MQKDLFQRAL NFRILNTKEI FRSSKDSYET
     FKAYVNDYSG FVLSCWCGSL NCENIIKNET KATIRCIPDD FKARDLTGMT CIYCSSKAKY
     FVLFAKSY