ID   ACYP_SALPA              Reviewed;          93 AA.
AC   Q5PGB8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=SPA1767;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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   -!- CAUTION: Lacks the conserved active site Arg in position 20. There is a
CC       histidine in this position. {ECO:0000305}.
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DR   EMBL; CP000026; AAV77684.1; -; Genomic_DNA.
DR   RefSeq; WP_000072878.1; NC_006511.1.
DR   AlphaFoldDB; Q5PGB8; -.
DR   SMR; Q5PGB8; -.
DR   EnsemblBacteria; AAV77684; AAV77684; SPA1767.
DR   KEGG; spt:SPA1767; -.
DR   HOGENOM; CLU_141932_1_2_6; -.
DR   OMA; VGFRWSM; -.
DR   Proteomes; UP000008185; 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; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase.
FT   CHAIN           1..93
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326796"
FT   DOMAIN          5..93
FT                   /note="Acylphosphatase-like"
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   93 AA;  10310 MW;  1FAF2C9C52E8AF77 CRC64;
     MSNVCIIAWV YGRVQGVGFH YTTQHEAQRL GLTGYAKNMD DGSVEVVACG DAAQVEKLIK
     WLKEGGPRSA RVDKILTEPH SPRETLTGFS IRY