ID   ACYP_ECOK1              Reviewed;          92 AA.
AC   A1A9N7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 77.
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}; OrderedLocusNames=Ecok1_08830;
GN   ORFNames=APECO1_73;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ00377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000468; ABJ00377.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000048217.1; NC_008563.1.
DR   AlphaFoldDB; A1A9N7; -.
DR   SMR; A1A9N7; -.
DR   EnsemblBacteria; ABJ00377; ABJ00377; APECO1_73.
DR   KEGG; ecv:APECO1_73; -.
DR   HOGENOM; CLU_1624530_0_0_6; -.
DR   Proteomes; UP000008216; Chromosome.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-UniRule.
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; PTHR47268; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; SSF54975; 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.
FT   CHAIN           1..92
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326708"
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;  10254 MW;  7BAAC1660C5EA2D6 CRC64;
     MSKVCIIAWI YGRVQGVGFR YTTQYEAKKL GLTGYAKNLD DGSVEVVACG DEGQVEKLIQ
     WLKSGGPRSA RVERVLSEPH HPSGELTDFR IR