ID   SYP_GLUOX               Reviewed;         438 AA.
AC   Q5FUU9;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=GOX0079;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000009; AAW59876.1; -; Genomic_DNA.
DR   RefSeq; WP_011251680.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FUU9; -.
DR   SMR; Q5FUU9; -.
DR   STRING; 290633.GOX0079; -.
DR   EnsemblBacteria; AAW59876; AAW59876; GOX0079.
DR   KEGG; gox:GOX0079; -.
DR   eggNOG; COG0442; Bacteria.
DR   HOGENOM; CLU_016739_4_2_5; -.
DR   OMA; NCDYAAN; -.
DR   Proteomes; UP000006375; 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; Reference proteome.
FT   CHAIN           1..438
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000248901"
SQ   SEQUENCE   438 AA;  48937 MW;  CE8EB125898E463E CRC64;
     MRLTKAFQPT LKEVPAEAQI ASHRLMLRAG LVRQTASGIY AWLPAGLRVL RNIEQIIREE
     QDAIGAQEVL MPTLQSAELW RRSGRYDAYG PEMLRIQDRH GRDLLYGPTN EEMITDIFGS
     SVKSYKELPK ALYHIQWKFR DEVRPRFGVM RGREFLMKDA YSFDASYEGA VASYRRMMLS
     YLRIFQRLGV RAVPMVADTG PIGGDLSHEF LVLAPTGESA VFFDAALEEQ DWLSRPVDCD
     DAESLATFFA TVTDHYAATD EKHDEAEWAK VPAERKREGR GIEVGHIFYF GTKYTASMGI
     EVSGPDGAPF HPHMGSYGVG VSRLVGAIIE ASHDDAGIIW PASVAPYRAA ILNLRQDDEA
     CDAICDRIYG TDPENLLYDD RSERAGVKFN DADLMGHPWQ IIVGPRGAKE GKVELKQRAT
     GERFELSVED ALAKIGAA