ID   BSHB2_BACCR             Reviewed;         220 AA.
AC   Q81AU5;
DT   27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
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:0000269|PubMed:23758290};
GN   Name=bshB2 {ECO:0000303|PubMed:23758290};
GN   Synonyms=bca {ECO:0000303|PubMed:23758290};
GN   OrderedLocusNames=BC_3461 {ECO:0000312|EMBL:AAP10396.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=23758290; DOI=10.1042/bj20130415;
RA   Fang Z., Roberts A.A., Weidman K., Sharma S.V., Claiborne A.,
RA   Hamilton C.J., Dos Santos P.C.;
RT   "Cross-functionalities of Bacillus deacetylases involved in bacillithiol
RT   biosynthesis and bacillithiol-S-conjugate detoxification pathways.";
RL   Biochem. J. 454:239-247(2013).
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       Has weak activity compared with bshB1. {ECO:0000269|PubMed:23758290}.
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:0000269|PubMed:23758290};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q81FP2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.21 mM for GlcNAc-Mal {ECO:0000269|PubMed:23758290};
CC         Note=kcat is 0.068 with GlcNAc-Mal. {ECO:0000269|PubMed:23758290};
CC   -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
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DR   EMBL; AE016877; AAP10396.1; -; Genomic_DNA.
DR   RefSeq; NP_833195.1; NC_004722.1.
DR   RefSeq; WP_000439483.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81AU5; -.
DR   SMR; Q81AU5; -.
DR   STRING; 226900.BC_3461; -.
DR   PRIDE; Q81AU5; -.
DR   EnsemblBacteria; AAP10396; AAP10396; BC_3461.
DR   GeneID; 67508103; -.
DR   KEGG; bce:BC3461; -.
DR   PATRIC; fig|226900.8.peg.3549; -.
DR   HOGENOM; CLU_049311_4_2_9; -.
DR   OMA; QHKTQAL; -.
DR   SABIO-RK; Q81AU5; -.
DR   Proteomes; UP000001417; 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   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..220
FT                   /note="Probable N-acetyl-alpha-D-glucosaminyl L-malate
FT                   deacetylase 2"
FT                   /id="PRO_0000433163"
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   220 AA;  24920 MW;  B56BED88B26BB65F CRC64;
     MERHVLVVFP HPDDEAYAAG GTIRLLTDQG VPVTYACGTL GQMGRNMGKN VFANRETIPH
     IRKKELKDAC EAMGIKDLRM LGFHDKTLEF EDVDFVADKI EAIIQEVNPS RIITFYPEHG
     VHPDHNAFGR AVVRAVSRMP KEERPVIHAV AITKNREAVL GEPDVVNNIS EVFDHKLTAL
     GAHRSQTEAM LEDTHAKIKN KDAATLKWLQ LEQFWTYKWE