BSHB2_BACSU
ID BSHB2_BACSU Reviewed; 221 AA.
AC O31857; C0SP96; Q7BV97;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable N-acetyl-alpha-D-glucosaminyl L-malate deacetylase 2 {ECO:0000305};
DE Short=GlcNAc-Mal deacetylase 2 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q81WT0};
GN Name=bshB2 {ECO:0000303|PubMed:20308541}; Synonyms=yojG;
GN OrderedLocusNames=BSU19460;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
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 SEQUENCE REVISION TO N-TERMINUS.
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).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=20308541; DOI=10.1073/pnas.1000928107;
RA Gaballa A., Newton G.L., Antelmann H., Parsonage D., Upton H., Rawat M.,
RA Claiborne A., Fahey R.C., Helmann J.D.;
RT "Biosynthesis and functions of bacillithiol, a major low-molecular-weight
RT thiol in Bacilli.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6482-6486(2010).
CC -!- FUNCTION: Involved in bacillithiol (BSH) biosynthesis. Catalyzes the
CC second step of the pathway, the deacetylation of N-
CC acetylglucosaminylmalate (GlcNAc-Mal) to glucosamine malate (GlcN-Mal).
CC {ECO:0000250|UniProtKB:Q81WT0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malyl N-acetyl-alpha-D-glucosaminide + H2O = (S)-malyl
CC alpha-D-glucosaminide + acetate; Xref=Rhea:RHEA:33411,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:64870,
CC ChEBI:CHEBI:64871; Evidence={ECO:0000250|UniProtKB:Q81WT0};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q81FP2};
CC -!- DISRUPTION PHENOTYPE: Mutant has normal levels of bacillithiol, but
CC bshB1/bshB2 double mutant does not produce bacillithiol.
CC {ECO:0000269|PubMed:20308541}.
CC -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17855.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF026147; AAC17855.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB13838.2; -; Genomic_DNA.
DR PIR; D69906; D69906.
DR RefSeq; WP_003231215.1; NZ_JNCM01000036.1.
DR RefSeq; YP_054582.2; NC_000964.3.
DR AlphaFoldDB; O31857; -.
DR SMR; O31857; -.
DR STRING; 224308.BSU19460; -.
DR PRIDE; O31857; -.
DR EnsemblBacteria; CAB13838; CAB13838; BSU_19460.
DR GeneID; 2914250; -.
DR KEGG; bsu:BSU19460; -.
DR PATRIC; fig|224308.179.peg.2128; -.
DR eggNOG; COG2120; Bacteria.
DR InParanoid; O31857; -.
DR OMA; QHKTQAL; -.
DR PhylomeDB; O31857; -.
DR BioCyc; BSUB:BSU19460-MON; -.
DR BioCyc; MetaCyc:BSU19460-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10320; -; 1.
DR InterPro; IPR023841; BshB2.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR PANTHER; PTHR12993; PTHR12993; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; SSF102588; 1.
DR TIGRFAMs; TIGR04000; thiol_BshB2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..221
FT /note="Probable N-acetyl-alpha-D-glucosaminyl L-malate
FT deacetylase 2"
FT /id="PRO_0000386549"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81FP2"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81FP2"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81FP2"
SQ SEQUENCE 221 AA; 25577 MW; AAED3A1832B35325 CRC64;
MKEHVLVILP HPDDESYGVA GLIALNRKKD IPVTYACATL GEMGRNMGDP FFANRETLPL
LRKQELINAC KEMDINDLRM LGLRDKTLEF EDDEYLADIM EEIIDDVKPS LIVTFYPGHG
VHPDHDACGE AVIRALYRKK KEDRPRTICM AITRNREEVL GEADVVLDIK EVADIKMNAL
RAHRTQTEGM LRELEEKLKN NEPVMATWFE EEIYWTYQWN D
