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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
 
 
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