BSHB1_BACSU
ID BSHB1_BACSU Reviewed; 236 AA.
AC P42981;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 121.
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:0000250|UniProtKB:Q81ST8};
GN Name=bshB1 {ECO:0000303|PubMed:20308541}; Synonyms=jojG, ypjG;
GN OrderedLocusNames=BSU22470;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
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 C-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:Q81ST8}.
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:Q81ST8};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q81FP2};
CC -!- DISRUPTION PHENOTYPE: Mutant shows a 2-fold reduction in bacillithiol
CC levels. BshB1/bshB2 double mutant does not produce bacillithiol.
CC {ECO:0000269|PubMed:20308541}.
CC -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
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DR EMBL; L38424; AAA92876.1; -; Genomic_DNA.
DR EMBL; L47709; AAB38444.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14163.2; -; Genomic_DNA.
DR PIR; F69937; F69937.
DR RefSeq; NP_390128.2; NC_000964.3.
DR RefSeq; WP_003230642.1; NZ_JNCM01000036.1.
DR RefSeq; WP_009967589.1; NZ_CM000487.1.
DR PDB; 6P2T; X-ray; 1.85 A; A=1-236.
DR PDB; 6ULL; X-ray; 1.45 A; A=1-236.
DR PDBsum; 6P2T; -.
DR PDBsum; 6ULL; -.
DR AlphaFoldDB; P42981; -.
DR SMR; P42981; -.
DR STRING; 224308.BSU22470; -.
DR PaxDb; P42981; -.
DR PRIDE; P42981; -.
DR EnsemblBacteria; CAB14163; CAB14163; BSU_22470.
DR GeneID; 939026; -.
DR KEGG; bsu:BSU22470; -.
DR PATRIC; fig|224308.179.peg.2451; -.
DR eggNOG; COG2120; Bacteria.
DR InParanoid; P42981; -.
DR OMA; EIVLCNA; -.
DR PhylomeDB; P42981; -.
DR BioCyc; BSUB:BSU22470-MON; -.
DR BioCyc; MetaCyc:BSU22470-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
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 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 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..236
FT /note="N-acetyl-alpha-D-glucosaminyl L-malate deacetylase
FT 1"
FT /id="PRO_0000049705"
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 CONFLICT 218..236
FT /note="GFFSKRMLMLDHDVLGGEQ -> VSFPNGC (in Ref. 1; AAB38444/
FT AAA92876)"
FT /evidence="ECO:0000305"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:6ULL"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:6ULL"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:6ULL"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6ULL"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:6ULL"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:6ULL"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:6ULL"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:6ULL"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6ULL"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:6ULL"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:6ULL"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6ULL"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6ULL"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:6ULL"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:6ULL"
FT TURN 191..195
FT /evidence="ECO:0007829|PDB:6ULL"
FT HELIX 196..210
FT /evidence="ECO:0007829|PDB:6ULL"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:6ULL"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:6ULL"
SQ SEQUENCE 236 AA; 26264 MW; 486F6FC5622A2B34 CRC64;
MYNADVLAFG AHSDDVEIGM GGTIAKFVKQ EKKVMICDLT EAELSSNGTV SLRKEEAAEA
ARILGADKRI QLTLPDRGLI MSDQAIRSIV TVIRICRPKA VFMPYKKDRH PDHGNAAALV
EEAIFSAGIH KYKDEKSLPA HKVSKVYYYM INGFHQPDFV IDISDTIEAK KQSLNAYKSQ
FIPSKDSVST PLTNGYIEIV EAREKLYGKE AGVEYAEGFF SKRMLMLDHD VLGGEQ