YHAA_BACSU
ID YHAA_BACSU Reviewed; 396 AA.
AC O07598; O07512;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative amidohydrolase YhaA;
DE EC=3.5.1.-;
GN Name=yhaA; OrderedLocusNames=BSU10070;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP SEQUENCE REVISION TO 89-92.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AL009126; CAB12847.2; -; Genomic_DNA.
DR RefSeq; NP_388888.2; NC_000964.3.
DR RefSeq; WP_003245681.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07598; -.
DR SMR; O07598; -.
DR STRING; 224308.BSU10070; -.
DR PaxDb; O07598; -.
DR PRIDE; O07598; -.
DR EnsemblBacteria; CAB12847; CAB12847; BSU_10070.
DR GeneID; 936299; -.
DR KEGG; bsu:BSU10070; -.
DR PATRIC; fig|224308.179.peg.1083; -.
DR eggNOG; COG1473; Bacteria.
DR InParanoid; O07598; -.
DR OMA; VMIHQHA; -.
DR PhylomeDB; O07598; -.
DR BioCyc; BSUB:BSU10070-MON; -.
DR BioCyc; MetaCyc:BSU10070-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR11014; PTHR11014; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE 3: Inferred from homology;
KW Cobalt; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..396
FT /note="Putative amidohydrolase YhaA"
FT /id="PRO_0000387968"
FT ACT_SITE 85
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 43220 MW; 15C28C35D411CA0A CRC64;
MSISTLQKEI NKQLDGCFEE MVEIRRHFHM YPELSFQEEK TAAFIASYYE SLGVPIRTNV
GGRGVLANIE GSEPGPTVAL RADFDALPIQ DEKDVPYASK VPGVMHACGH DGHTAALLAV
AKVLHQNRHE LKGTFVMIHQ HAEEYYPGGA KPMIDDGCLE NTDVIFGTHL WATEPLGTIL
CRPGAVMAAA DRFTIKVFGK GGHGAHPHDT KDAVLIGSQI VSSLQHIVSR KVNPIQSAVI
STGSFIADNP FNVIADQAVL IGTARSFDEN VRDILEKEIE AVVKGICSMH GASYEYTYEQ
GYPAVVNHPA ETNHLVSTAK NTEGVQQVID GEPQMGGEDF AYYLQNVKGT FFFTGAAPEQ
PERVYSHHHP KFDINEKAML TAAKVLAGAA ITYHQL
