ID   PDUW_ESCF3              Reviewed;         404 AA.
AC   B7LTX5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=EFER_2027;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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}.
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DR   EMBL; CU928158; CAQ89532.1; -; Genomic_DNA.
DR   RefSeq; WP_000018485.1; NC_011740.1.
DR   AlphaFoldDB; B7LTX5; -.
DR   SMR; B7LTX5; -.
DR   EnsemblBacteria; CAQ89532; CAQ89532; EFER_2027.
DR   GeneID; 60900818; -.
DR   KEGG; efe:EFER_2027; -.
DR   HOGENOM; CLU_020352_0_1_6; -.
DR   OMA; PLPWRYY; -.
DR   OrthoDB; 537106at2; -.
DR   BioCyc; EFER585054:EFER_RS10185-MON; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000000745; 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_0000398198"
SQ   SEQUENCE   404 AA;  43912 MW;  F59A8C873AF7A25C CRC64;
     MSHKIMAINA GSSSLKFQLL AMPEGEILCQ GIIERIGLAD ARLVVKTATE KWQEITPVAD
     HREAVTLLLE QLINRKIINS LHDIDATGHR VAHGGETFKD SALVTDDVMA EIERLAELAP
     LHNPVNLLGI NIFRQLLPSA PTIAVFDTAF HQTLEMPAYI YPLPWRYYHE LGIRRYGFHG
     TSHKYVSGKL AEKLGVPLSA LRVVCCHLGN GSSVCAIKGG KSVNTSMGFT PQSGVMMGTR
     SGDIDPSILP WIALREGKTP QELNQLLNNE SGLLGVSGVS PDFRDIEQAA ENGNQQAQLA
     LALFAERIRA TIGSYVLQMG GLDALIFTGG IGENSARARA AICNNLHFLG LSIDADKNQH
     NATFIQSEQA MVKVAVINTN EELMIARDVM RIALPEPALQ EVLA