BSHB1_BACAN
ID BSHB1_BACAN Reviewed; 234 AA.
AC Q81ST8; E9QQT9; E9QQU0; Q6I118; Q6KUX1;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=N-acetyl-alpha-D-glucosaminyl L-malate deacetylase 1 {ECO:0000305};
DE Short=GlcNAc-Mal deacetylase 1 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000269|PubMed:20308541};
GN Name=bshB1 {ECO:0000303|PubMed:20308541};
GN Synonyms=bshB {ECO:0000303|PubMed:23758290};
GN OrderedLocusNames=BA_1557 {ECO:0000312|EMBL:AAP25493.1},
GN BAS1444 {ECO:0000312|EMBL:AAT53764.1},
GN GBAA_1557 {ECO:0000312|EMBL:AAT30655.1};
GN ORFNames=BF27_424 {ECO:0000312|EMBL:AJH90866.1},
GN TM00_07895 {ECO:0000312|EMBL:AJG28381.1};
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2002013094;
RA Davenport K.W., Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O.,
RA Coyne S.R., Daligault H.E., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pollino;
RA Fasanella A., Braun P., Grass G., Hanczaruk M., Aceti A., Serrecchia L.,
RA Marino L., Georgi E., Antwerpen M.H.;
RT "Genome sequence of Bacillus anthracis Pollino isolated from a bovine
RT anthrax-burial site in Italy.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Sterne;
RX PubMed=20799687; DOI=10.1021/bi100698n;
RA Parsonage D., Newton G.L., Holder R.C., Wallace B.D., Paige C.,
RA Hamilton C.J., Dos Santos P.C., Redinbo M.R., Reid S.D., Claiborne A.;
RT "Characterization of the N-acetyl-alpha-D-glucosaminyl L-malate synthase
RT and deacetylase functions for bacillithiol biosynthesis in Bacillus
RT anthracis.";
RL Biochemistry 49:8398-8414(2010).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-14; ARG-53; ARG-109
RP AND HIS-110.
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 {ECO:0000269|PubMed:20308541, ECO:0000269|PubMed:20799687,
CC 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:20308541,
CC ECO:0000269|PubMed:20799687, ECO:0000269|PubMed:23758290};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23758290};
CC Note=Can also use Ni(2+), Co(2+) and Fe(3+).
CC {ECO:0000269|PubMed:23758290};
CC -!- ACTIVITY REGULATION: Inhibited by BSH. {ECO:0000269|PubMed:23758290}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for GlcNAc-Mal {ECO:0000269|PubMed:20799687};
CC KM=0.19 mM for GlcNAc-Mal {ECO:0000269|PubMed:23758290};
CC KM=57.1 mM for GlcNAc {ECO:0000269|PubMed:23758290};
CC KM=0.48 mM for BSH {ECO:0000269|PubMed:23758290};
CC KM=0.32 mM for bacillithiol-S-bimane (BSmB)
CC {ECO:0000269|PubMed:23758290};
CC Note=kcat is 42 sec(-1) with GlcNAc-Mal (PubMed:20799687). kcat is
CC 8.24 sec(-1) with GlcNAc-Mal (PubMed:23758290).
CC {ECO:0000269|PubMed:20799687, ECO:0000269|PubMed:23758290};
CC -!- DISRUPTION PHENOTYPE: Deletion reduces bacillithiol levels by 30%.
CC {ECO:0000269|PubMed:20799687}.
CC -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
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DR EMBL; AE016879; AAP25493.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30655.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53764.1; -; Genomic_DNA.
DR EMBL; CP009902; AJH90866.1; -; Genomic_DNA.
DR EMBL; CP010813; AJG28381.1; -; Genomic_DNA.
DR RefSeq; NP_844007.1; NC_003997.3.
DR RefSeq; WP_000015666.1; NZ_WXXJ01000001.1.
DR RefSeq; YP_027713.1; NC_005945.1.
DR AlphaFoldDB; Q81ST8; -.
DR SMR; Q81ST8; -.
DR STRING; 261594.GBAA_1557; -.
DR DNASU; 1087010; -.
DR EnsemblBacteria; AAP25493; AAP25493; BA_1557.
DR EnsemblBacteria; AAT30655; AAT30655; GBAA_1557.
DR GeneID; 45021529; -.
DR KEGG; ban:BA_1557; -.
DR KEGG; bar:GBAA_1557; -.
DR KEGG; bat:BAS1444; -.
DR PATRIC; fig|198094.11.peg.1527; -.
DR eggNOG; COG2120; Bacteria.
DR HOGENOM; CLU_049311_3_1_9; -.
DR OMA; EIVLCNA; -.
DR SABIO-RK; Q81ST8; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071793; P:bacillithiol biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.10320; -; 1.
DR InterPro; IPR023842; Bacillithiol_biosynth_BshB1.
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; TIGR04001; thiol_BshB1; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..234
FT /note="N-acetyl-alpha-D-glucosaminyl L-malate deacetylase
FT 1"
FT /id="PRO_0000433160"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81FP2"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81FP2"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81FP2"
FT MUTAGEN 14
FT /note="D->A: 3000-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:23758290"
FT MUTAGEN 53
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:23758290"
FT MUTAGEN 53
FT /note="R->K: Strong decrease in activity for GlcNAc-Mal. No
FT activity with GlcNAc."
FT /evidence="ECO:0000269|PubMed:23758290"
FT MUTAGEN 109
FT /note="R->K: 6-fold decrease in kcat with GlcNAc-Mal."
FT /evidence="ECO:0000269|PubMed:23758290"
FT MUTAGEN 110
FT /note="H->A: 4-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:23758290"
SQ SEQUENCE 234 AA; 26199 MW; 8F84AF35474DDA27 CRC64;
MSGLHILAFG AHADDVEIGM AGTIAKYTKQ GYEVGICDLT EADLSSNGTI ELRKEEAKAA
ARIMGVKTRL NLAMPDRGLY MKEEYIREIV KVIRTYKPKL VFAPYYEDRH PDHANCAKLV
EEAIFSAGIR KYMPEVPPHR VESFYHYMIN GFHKPNFCID ISEYVSQKVE ALEAYESQFS
TGSDGVKTPL TEGYVETVVA REKMFGKEVG VLYAEGFMSK KPVLLHADLI GGCK
