ID   EUTP_SALTI              Reviewed;         159 AA.
AC   P0A209; Q9ZFV6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Probable acetate kinase EutP;
DE            EC=2.7.2.1 {ECO:0000250|UniProtKB:P0A208};
DE   AltName: Full=Ethanolamine utilization protein EutP;
GN   Name=eutP; OrderedLocusNames=STY2705, t0390;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: A putative bidirectional acetate kinase that may drive flux
CC       through the ethanolamine degradation pathway under anoxic conditions
CC       found when this bacteria infects host intestine. It may generate ATP
CC       that can be used by other enzymes (EutA and EutT) in the eut pathway.
CC       {ECO:0000250|UniProtKB:P0A208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC         ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; EC=2.7.2.1;
CC         Evidence={ECO:0000250|UniProtKB:P0A208};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11353;
CC         Evidence={ECO:0000250|UniProtKB:P0A208};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11354;
CC         Evidence={ECO:0000250|UniProtKB:P0A208};
CC   -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000250|UniProtKB:P0A208}.
CC   -!- SIMILARITY: Belongs to the EutP/PduV family. {ECO:0000305}.
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DR   EMBL; AL513382; CAD07699.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68108.1; -; Genomic_DNA.
DR   RefSeq; NP_457003.1; NC_003198.1.
DR   RefSeq; WP_000820751.1; NZ_WSUR01000025.1.
DR   AlphaFoldDB; P0A209; -.
DR   STRING; 220341.16503685; -.
DR   EnsemblBacteria; AAO68108; AAO68108; t0390.
DR   KEGG; stt:t0390; -.
DR   KEGG; sty:STY2705; -.
DR   PATRIC; fig|220341.7.peg.2742; -.
DR   eggNOG; COG4917; Bacteria.
DR   HOGENOM; CLU_113298_2_0_6; -.
DR   OMA; PGEYMEN; -.
DR   UniPathway; UPA00560; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR012381; EutP_PduV.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR40453; PTHR40453; 1.
DR   Pfam; PF10662; PduV-EutP; 1.
DR   PIRSF; PIRSF036409; EutP_PduV; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02528; EutP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bacterial microcompartment; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..159
FT                   /note="Probable acetate kinase EutP"
FT                   /id="PRO_0000087095"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   159 AA;  17726 MW;  C674D376409FAA83 CRC64;
     MKRIAFVGAV GAGKTTLFNA LRGNYSLARK TQAVEFNDHG DIDTPGEYFS HPRWYHALIT
     TLQDVDTLIY VHAANDKESR LPAGLLDVGT RKRHIAVISK TDMPDADVAA TRQLLCEIGF
     REPIFELNGH DPQSVRQLVD YLAALSEQEE EAGEKTYHS