ID   SYP_BACTN               Reviewed;         497 AA.
AC   Q8A988;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01571};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01571};
DE            Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01571};
GN   Name=proS {ECO:0000255|HAMAP-Rule:MF_01571}; OrderedLocusNames=BT_0929;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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_01571}.
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_01571};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       anticodon-binding domain and the C-terminal extension.
CC       {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571}.
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DR   EMBL; AE015928; AAO76036.1; -; Genomic_DNA.
DR   RefSeq; NP_809842.1; NC_004663.1.
DR   RefSeq; WP_011107525.1; NZ_UYXG01000013.1.
DR   AlphaFoldDB; Q8A988; -.
DR   SMR; Q8A988; -.
DR   STRING; 226186.BT_0929; -.
DR   PaxDb; Q8A988; -.
DR   PRIDE; Q8A988; -.
DR   EnsemblBacteria; AAO76036; AAO76036; BT_0929.
DR   GeneID; 60926903; -.
DR   KEGG; bth:BT_0929; -.
DR   PATRIC; fig|226186.12.peg.943; -.
DR   eggNOG; COG0442; Bacteria.
DR   HOGENOM; CLU_001882_4_2_10; -.
DR   InParanoid; Q8A988; -.
DR   OMA; EVYWVTH; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
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; 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   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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000249123"
SQ   SEQUENCE   497 AA;  56848 MW;  5960D3C9344E11FA CRC64;
     MAKELKDLTK RSENYSQWYN DLVVKADLAE QSAVRGCMVI KPYGYAIWEK MQRQLDDMFK
     ETGHVNAYFP LLIPKSFLSR EAEHVEGFAK ECAVVTHYRL KNAEDGSGVV VDPAAKLEEE
     LIIRPTSETI IWNTYKNWIQ SYRDLPILCN QWANVFRWEM RTRLFLRTAE FLWQEGHTAH
     ATREEAEEEA IRMLNVYGEF AEKYMAVPVV KGVKSANERF AGALDTYTIE AMMQDGKALQ
     SGTSHFLGQN FAKAFDVQFV NKENKMEYVW ATSWGVSTRL MGALIMTHSD DNGLVLPPHL
     APIQVVIVPI YKNDEQLKQI DAKVEGIVAK LKALGISVKY DNADNKRPGF KFADYELKGV
     PVRLVMGGRD LENNTMEVMR RDTLEKETVT CDGIETYVQK LLEEIQANIY KKALDYRNSK
     ITTVDTYEEF KEKIEEGGFI LAHWDGTTET EEKIKEDTKA TIRCIPFDSY VEGDKEPGKC
     MVTGKPSACR VVFARSY