PDUW_SALTY
ID PDUW_SALTY Reviewed; 404 AA.
AC P74879; Q9XDM5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Propionate kinase PduW {ECO:0000255|HAMAP-Rule:MF_01882, ECO:0000303|PubMed:12700259};
DE EC=2.7.2.15 {ECO:0000255|HAMAP-Rule:MF_01882, ECO:0000305|PubMed:12700259};
GN Name=pduW {ECO:0000255|HAMAP-Rule:MF_01882, ECO:0000303|PubMed:10498708};
GN OrderedLocusNames=STM2057;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=23566;
RA Denduangboripant J., Panbangred W.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=10498708; DOI=10.1128/jb.181.19.5967-5975.1999;
RA Bobik T.A., Havemann G.D., Busch R.J., Williams D.S., Aldrich H.C.;
RT "The propanediol utilization (pdu) operon of Salmonella enterica serovar
RT typhimurium LT2 includes genes necessary for formation of polyhedral
RT organelles involved in coenzyme B(12)-dependent 1, 2-propanediol
RT degradation.";
RL J. Bacteriol. 181:5967-5975(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=12700259; DOI=10.1128/jb.185.9.2802-2810.2003;
RA Palacios S., Starai V.J., Escalante-Semerena J.C.;
RT "Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and
RT propionate catabolic pathways needed for expression of the prpBCDE operon
RT during growth of Salmonella enterica on 1,2-propanediol.";
RL J. Bacteriol. 185:2802-2810(2003).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=26448059; DOI=10.1111/mmi.13243;
RA Moore T.C., Escalante-Semerena J.C.;
RT "The EutQ and EutP proteins are novel acetate kinases involved in
RT ethanolamine catabolism: physiological implications for the function of the
RT ethanolamine metabolosome in Salmonella enterica.";
RL Mol. Microbiol. 99:497-511(2016).
CC -!- FUNCTION: Works with phosphate acetyltransferase (pta) to capture
CC exogenous propionate and regenerate propionyl-CoA during degradation of
CC propionate and 1,2-propanediol (1,2-PD). Ectopic expression partially
CC complements a cobB deletion allowing some growth on propionate
CC (PubMed:12700259). Restores growth to an eutQ deletion on ethanolamine
CC and tetrathionate under anoxic conditions (PubMed:26448059).
CC {ECO:0000269|PubMed:12700259, ECO:0000269|PubMed:26448059}.
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 ECO:0000305|PubMed:12700259};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000269|PubMed:12700259, ECO:0000305|PubMed:10498708}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000269|PubMed:12700259}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01882,
CC ECO:0000305|PubMed:26448059}.
CC -!- INDUCTION: The BMC operon and BMC production is induced by growth on
CC 1,2-PD vitamin B12 medium. {ECO:0000269|PubMed:10498708}.
CC -!- DISRUPTION PHENOTYPE: Decreased propionate kinase activity, cells grow
CC to lower density on 1,2-PD and excrete more propionate into the medium.
CC A double pduW-pduX deletion grows as well as wild-type on 1,2-PD.
CC {ECO:0000269|PubMed:12700259}.
CC -!- SIMILARITY: Belongs to the acetokinase family. PduW subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01882}.
CC -!- CAUTION: Was originally (Ref.1) thought to be AckA. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39021.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U67435; AAB09552.1; -; Genomic_DNA.
DR EMBL; AF026270; AAD39021.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL20961.1; -; Genomic_DNA.
DR RefSeq; NP_461002.1; NC_003197.2.
DR RefSeq; WP_000120647.1; NC_003197.2.
DR AlphaFoldDB; P74879; -.
DR SMR; P74879; -.
DR STRING; 99287.STM2057; -.
DR PaxDb; P74879; -.
DR EnsemblBacteria; AAL20961; AAL20961; STM2057.
DR GeneID; 1253578; -.
DR KEGG; stm:STM2057; -.
DR PATRIC; fig|99287.12.peg.2179; -.
DR HOGENOM; CLU_020352_0_1_6; -.
DR OMA; PLPWRYY; -.
DR PhylomeDB; P74879; -.
DR BioCyc; MetaCyc:STM2057-MON; -.
DR BioCyc; SENT99287:STM2057-MON; -.
DR UniPathway; UPA00621; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008776; F:acetate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008980; F:propionate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006083; P:acetate metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..404
FT /note="Propionate kinase PduW"
FT /id="PRO_0000107651"
FT CONFLICT 25
FT /note="G -> R (in Ref. 1; AAB09552)"
FT /evidence="ECO:0000305"
FT CONFLICT 60..67
FT /note="DHRDAVTL -> RSSRCVNW (in Ref. 1; AAB09552)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="A -> R (in Ref. 1; AAB09552)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="S -> T (in Ref. 1; AAB09552)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..261
FT /note="SILPWIAQRESKTPQ -> HSAVDSPARNENAE (in Ref. 1;
FT AAB09552)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..309
FT /note="ALTLFAERIR -> RSHSVCRTHS (in Ref. 1; AAB09552)"
FT /evidence="ECO:0000305"
FT CONFLICT 342..352
FT /note="VCHNLQFLGLA -> CAIISIFGLS (in Ref. 1; AAB09552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 43995 MW; E236F981EAFBB304 CRC64;
MSYKIMAINA GSSSLKFQLL EMPQGDMLCQ GLIERIGMAD AQVTIKTHSQ KWQETVPVAD
HRDAVTLLLE KLLGYQIINS LRDIDGVGHR VAHGGEFFKD STLVTDETLA QIERLAELAP
LHNPVNALGI HVFRQLLPDA PSVAVFDTAF HQTLDEPAYI YPLPWHYYAE LGIRRYGFHG
TSHKYVSGVL AEKLGVPLSA LRVICCHLGN GSSICAIKNG RSVNTSMGFT PQSGVMMGTR
SGDIDPSILP WIAQRESKTP QQLNQLLNNE SGLLGVSGVS SDYRDVEQAA NTGNRQAKLA
LTLFAERIRA TIGSYIMQMG GLDALVFTGG IGENSARARS AVCHNLQFLG LAVDEEKNQR
NATFIQTENA LVKVAVINTN EELMIAQDVM RIALPATEGL CVPA
