ID   PDUW_SALPC              Reviewed;         404 AA.
AC   C0Q1L8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Propionate kinase {ECO:0000255|HAMAP-Rule:MF_01882};
DE            EC=2.7.2.15 {ECO:0000255|HAMAP-Rule:MF_01882};
GN   Name=pduW {ECO:0000255|HAMAP-Rule:MF_01882}; OrderedLocusNames=SPC_1657;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
CC   -!- FUNCTION: Works with phosphate acetyltransferase (pta) to capture
CC       exogenous propionate and regenerate propionyl-CoA during degradation of
CC       1,2-propanediol (1,2-PD). {ECO:0000250|UniProtKB:P74879}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + propanoate = ADP + propanoyl phosphate;
CC         Xref=Rhea:RHEA:23148, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58933, ChEBI:CHEBI:456216; EC=2.7.2.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01882};
CC   -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC       {ECO:0000250|UniProtKB:P74879, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01882}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. PduW subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01882}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACN45804.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000857; ACN45804.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000120654.1; NC_012125.1.
DR   AlphaFoldDB; C0Q1L8; -.
DR   SMR; C0Q1L8; -.
DR   EnsemblBacteria; ACN45804; ACN45804; SPC_1657.
DR   KEGG; sei:SPC_1657; -.
DR   HOGENOM; CLU_020352_0_1_6; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000001599; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008980; F:propionate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019543; P:propionate catabolic process; IEA:InterPro.
DR   HAMAP; MF_00020; Acetate_kinase; 1.
DR   HAMAP; MF_01882; Propion_kin_subfam2; 1.
DR   InterPro; IPR004372; Ac/propionate_kinase.
DR   InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR   InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR024896; Propionate_kinase_PduW.
DR   PANTHER; PTHR21060; PTHR21060; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR00016; ackA; 1.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..404
FT                   /note="Propionate kinase"
FT                   /id="PRO_0000398201"
SQ   SEQUENCE   404 AA;  44030 MW;  5E5F87899FF6CA92 CRC64;
     MSYKIMAINA GSSSLKFQLL EMPQGDMLCQ GLIERIGMAD AQVTIKTHSQ KWQETVPVAD
     HRDAVTLLLE KLLGYQIINS LRDIDGVGHR VAHGGEFFKD STLVTDETLA QIERLAELAP
     LHNPVNALGI HVFRQLLPDA PSVAVFDTAF HQTLDEPTYI YPLPWRYYAE LGIRRYGFHG
     TSHKYVSGVL AEKLGVPLSA LRVICCHLGN GSSICAIKNG RSVNTSMGFT PQSGVMMGTR
     SGDIDPSILP WIAQRESKTP QQLNQLLNNE SGLLGVSGVS SDYRDVEQAA NTGNRQAKLA
     LTLFAERIRA TIGSYIMQMG GLDALVFTGG VGENSARARS AVCHNLQFLG LAVDEEKNQR
     NATFIQTENA LVKVAVINTN EELMIAQDVM RIALPATEGL CVPA