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SYP_ZYMMO
ID   SYP_ZYMMO               Reviewed;         443 AA.
AC   P0DJA8; P75000; Q5NQC1;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 48.
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=ZMO0460;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=19816441; DOI=10.1038/nbt1009-893;
RA   Yang S., Pappas K.M., Hauser L.J., Land M.L., Chen G.L., Hurst G.B.,
RA   Pan C., Kouvelis V.N., Typas M.A., Pelletier D.A., Klingeman D.M.,
RA   Chang Y.J., Samatova N.F., Brown S.D.;
RT   "Improved genome annotation for Zymomonas mobilis.";
RL   Nat. Biotechnol. 27:893-894(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). {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; AE008692; AAV89084.2; -; Genomic_DNA.
DR   RefSeq; WP_011240369.1; NZ_CP035711.1.
DR   AlphaFoldDB; P0DJA8; -.
DR   SMR; P0DJA8; -.
DR   STRING; 264203.ZMO0460; -.
DR   EnsemblBacteria; AAV89084; AAV89084; ZMO0460.
DR   GeneID; 58026299; -.
DR   KEGG; zmo:ZMO0460; -.
DR   eggNOG; COG0442; Bacteria.
DR   HOGENOM; CLU_016739_4_2_5; -.
DR   OMA; NCDYAAN; -.
DR   OrthoDB; 665824at2; -.
DR   Proteomes; UP000001173; 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..443
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000139349"
SQ   SEQUENCE   443 AA;  50314 MW;  1C99624CDAB31587 CRC64;
     MRLSRYFLPV MKETPADAQI ISHKLMLRAG MIRQTAAGIY AWLPLGLRVL RRIEKIIREE
     QARAGALELL MPTLQTADLW RESGRYDAYG PEMLRIKDRH NRELLYGPTN EEMITALIRD
     NLQSYRDLPR IFYHIQWKFR DEVRPRFGVM RGREFLMKDA YSFDIDETAG RHNYNRMFVA
     YLNSFSRLGL RAIPMQADTG PIGGDLSHEF IVLAPNGESD VFYHSNWEQP TRHIEADFDD
     PKALQSIVND HISDYAATDE KRDPLREAQA GDKLRQSRGI EVGHIFFFGT KYSKPMGFTL
     PGPDGKPIPI QMGSYGIGIS RLLGAIIEAS HDDNGIIWPE AVAPYHVGLI NLRIDDENCR
     AIADSLYQRL EAAGIDTLYD DRNERGGAKF ATMDLIGLPW QVVIGPKGAE KGVVELKNRA
     NGEKQTISVE NAFNLLTAGH QQR
 
 
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