ID ACYP_BACSU Reviewed; 91 AA.
AC O35031;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; Synonyms=AcP, yflL; OrderedLocusNames=BSU07640;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=9272861; DOI=10.1016/s0378-1119(97)00130-3;
RA Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT "Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of
RT the Bacillus subtilis genome reveal genes for a new two-component system,
RT three spore germination proteins, an iron uptake system and a general
RT stress response protein.";
RL Gene 194:191-199(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP STRUCTURE BY NMR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVE SITE.
RX PubMed=20447399; DOI=10.1016/j.febslet.2010.04.069;
RA Hu J., Li D., Su X.D., Jin C., Xia B.;
RT "Solution structure and conformational heterogeneity of acylphosphatase
RT from Bacillus subtilis.";
RL FEBS Lett. 584:2852-2856(2010).
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:0000269|PubMed:20447399};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.3. {ECO:0000269|PubMed:20447399};
CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D86417; BAA22305.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12593.1; -; Genomic_DNA.
DR PIR; B69811; B69811.
DR RefSeq; NP_388645.1; NC_000964.3.
DR RefSeq; WP_003243829.1; NZ_JNCM01000032.1.
DR PDB; 2FHM; NMR; -; A=1-91.
DR PDB; 2HLT; NMR; -; A=1-91.
DR PDB; 2HLU; NMR; -; A=1-91.
DR PDB; 3BR8; X-ray; 1.33 A; A=1-91.
DR PDBsum; 2FHM; -.
DR PDBsum; 2HLT; -.
DR PDBsum; 2HLU; -.
DR PDBsum; 3BR8; -.
DR AlphaFoldDB; O35031; -.
DR BMRB; O35031; -.
DR SMR; O35031; -.
DR STRING; 224308.BSU07640; -.
DR PaxDb; 224308-BSU07640; -.
DR EnsemblBacteria; CAB12593; CAB12593; BSU_07640.
DR GeneID; 939684; -.
DR KEGG; bsu:BSU07640; -.
DR PATRIC; fig|224308.179.peg.830; -.
DR eggNOG; COG1254; Bacteria.
DR InParanoid; O35031; -.
DR OrthoDB; 9808093at2; -.
DR PhylomeDB; O35031; -.
DR BioCyc; BSUB:BSU07640-MONOMER; -.
DR EvolutionaryTrace; O35031; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..91
FT /note="Acylphosphatase"
FT /id="PRO_0000158552"
FT DOMAIN 3..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520,
FT ECO:0000269|PubMed:20447399"
FT ACT_SITE 36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520,
FT ECO:0000269|PubMed:20447399"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:3BR8"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3BR8"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:3BR8"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3BR8"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3BR8"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:3BR8"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:3BR8"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3BR8"
SQ SEQUENCE 91 AA; 10318 MW; 50795631BF3310F4 CRC64;
MLQYRIIVDG RVQGVGFRYF VQMEADKRKL AGWVKNRDDG RVEILAEGPE NALQSFVEAV
KNGSPFSKVT DISVTESRSL EGHHRFSIVY S
//
