SYP_ZYMMA
ID SYP_ZYMMA Reviewed; 443 AA.
AC F8DT95; P75000; Q5NQC1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 50.
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=Zmob_0991;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 /
OS NCIMB 8938 / NRRL B-806 / ZM1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=555217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC B-806 / ZM1;
RX PubMed=8661924; DOI=10.1007/s002030050334;
RA Peekhaus N., Kramer R.;
RT "The gluEMP operon from Zymomonas mobilis encodes a high-affinity glutamate
RT carrier with similarity to binding-protein-dependent transport systems.";
RL Arch. Microbiol. 165:325-332(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC B-806 / ZM1;
RX PubMed=21725006; DOI=10.1128/jb.05395-11;
RA Pappas K.M., Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., Detter C.,
RA Balakireva M., Han C.S., Savvakis G., Kyrpides N.C., Typas M.A.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. mobilis
RT lectotype strain ATCC 10988.";
RL J. Bacteriol. 193:5051-5052(2011).
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; X84019; CAA58846.1; -; Genomic_DNA.
DR EMBL; CP002850; AEH62826.1; -; Genomic_DNA.
DR RefSeq; WP_012817305.1; NC_017262.1.
DR AlphaFoldDB; F8DT95; -.
DR SMR; F8DT95; -.
DR STRING; 555217.Zmob_0991; -.
DR EnsemblBacteria; AEH62826; AEH62826; Zmob_0991.
DR KEGG; zmm:Zmob_0991; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_016739_4_2_5; -.
DR OMA; NCDYAAN; -.
DR Proteomes; UP000001494; 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..443
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000414238"
FT CONFLICT 37
FT /note="A -> S (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..53
FT /note="RRI -> GRN (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="L -> A (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="R -> P (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="I -> F (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="R -> C (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="D -> H (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 126..130
FT /note="RDLPR -> AILAG (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="A -> G (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..220
FT /note="SD -> RH (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="V -> I (in Ref. 1; CAA58846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 50288 MW; 3199624CD211005D 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
SGEKQTISVE DAFNLLTAGH QQR
