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Database: UniProt
Entry: P0AB66
LinkDB: P0AB66
Original site: P0AB66 
ID   ACYP_ECO57              Reviewed;          92 AA.
AC   P0AB66; P75877; Q9R7Q1;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Acylphosphatase {ECO:0000255|HAMAP-Rule:MF_01450};
DE            EC=3.6.1.7 {ECO:0000255|HAMAP-Rule:MF_01450};
DE   AltName: Full=Acylphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01450};
GN   Name=yccX {ECO:0000255|HAMAP-Rule:MF_01450};
GN   OrderedLocusNames=Z1320, ECs1052;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01450};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01450}.
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DR   EMBL; AE005174; AAG55454.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34475.1; -; Genomic_DNA.
DR   PIR; B85624; B85624.
DR   PIR; D90760; D90760.
DR   RefSeq; NP_309079.1; NC_002695.1.
DR   RefSeq; WP_000048252.1; NZ_VOAI01000006.1.
DR   AlphaFoldDB; P0AB66; -.
DR   BMRB; P0AB66; -.
DR   SMR; P0AB66; -.
DR   STRING; 155864.Z1320; -.
DR   GeneID; 75204059; -.
DR   GeneID; 916920; -.
DR   KEGG; ece:Z1320; -.
DR   KEGG; ecs:ECs_1052; -.
DR   PATRIC; fig|386585.9.peg.1177; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_1_2_6; -.
DR   OMA; VGFRWSM; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.100; -; 1.
DR   HAMAP; MF_01450; Acylphosphatase_entero; 1.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR028627; Acylphosphatase_bac.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   PANTHER; PTHR47268; ACYLPHOSPHATASE; 1.
DR   PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Reference proteome.
FT   CHAIN           1..92
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000158554"
FT   DOMAIN          5..92
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT   ACT_SITE        20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT   DISULFID        5..49
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
SQ   SEQUENCE   92 AA;  10300 MW;  C39D3D145598D873 CRC64;
     MSKVCIIAWV YGRVQGVGFR YTTQYEAKRL GLTGYAKNLD DGSVEVVACG EEGQVEKLMQ
     WLKSGGPRSA RVERVLSEPH HPSGELTDFR IR
//
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