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Database: UniProt
Entry: D4G6C4_BACNB
LinkDB: D4G6C4_BACNB
Original site: D4G6C4_BACNB 
ID   D4G6C4_BACNB            Unreviewed;       102 AA.
AC   D4G6C4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 2.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Acylphosphatase {ECO:0000256|ARBA:ARBA00015991, ECO:0000256|PROSITE-ProRule:PRU00520};
DE            EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
GN   Name=yflL {ECO:0000313|EMBL:BAI84280.2};
GN   ORFNames=BSNT_07142 {ECO:0000313|EMBL:BAI84280.2};
OS   Bacillus subtilis subsp. natto (strain BEST195).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=645657 {ECO:0000313|EMBL:BAI84280.2, ECO:0000313|Proteomes:UP000006805};
RN   [1] {ECO:0000313|EMBL:BAI84280.2, ECO:0000313|Proteomes:UP000006805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEST195 {ECO:0000313|EMBL:BAI84280.2,
RC   ECO:0000313|Proteomes:UP000006805};
RX   PubMed=20398357; DOI=10.1186/1471-2164-11-243;
RA   Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., Fujiyama A.,
RA   Itaya M., Sakakibara Y.;
RT   "Whole genome assembly of a natto production strain Bacillus subtilis natto
RT   from very short read data.";
RL   BMC Genomics 11:243-243(2010).
RN   [2] {ECO:0000313|EMBL:BAI84280.2, ECO:0000313|Proteomes:UP000006805}
RP   GENOME REANNOTATION.
RC   STRAIN=BEST195 {ECO:0000313|EMBL:BAI84280.2,
RC   ECO:0000313|Proteomes:UP000006805};
RX   PubMed=25329997; DOI=10.1371/journal.pone.0109999;
RA   Kamada M., Hase S., Sato K., Toyoda A., Fujiyama A., Sakakibara Y.;
RT   "Whole genome complete resequencing of Bacillus subtilis natto by combining
RT   long reads with high-quality short reads.";
RL   PLoS ONE 9:E109999-E109999(2014).
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:0000256|ARBA:ARBA00000744, ECO:0000256|PROSITE-
CC         ProRule:PRU00520, ECO:0000256|RuleBase:RU000553};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005614, ECO:0000256|RuleBase:RU004168}.
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DR   EMBL; AP011541; BAI84280.2; -; Genomic_DNA.
DR   AlphaFoldDB; D4G6C4; -.
DR   STRING; 86029.AWV81_04200; -.
DR   KEGG; bso:BSNT_07142; -.
DR   HOGENOM; CLU_141932_2_0_9; -.
DR   Proteomes; UP000006805; Chromosome.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
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   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520,
KW   ECO:0000256|RuleBase:RU000553}.
FT   DOMAIN          14..101
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   ACT_SITE        29
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   102 AA;  11624 MW;  6E8464357E641D99 CRC64;
     MIIIKRKGGF YMLQYRIIVN GRVQGVGFRY FVQMEADKRK LAGWVKNRDD GRVEILAEGP
     ENALQSFVEA VKNGSPFSKV TDISVTESRS LEGHHRFSIV YS
//
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