CHBG_KLEP7
ID CHBG_KLEP7 Reviewed; 252 AA.
AC A6T7U7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE Short=COD {ECO:0000255|HAMAP-Rule:MF_01246};
DE EC=3.5.1.105 {ECO:0000255|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitin disaccharide deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitobiose deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitobiose-6P deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitotriose deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitotriose-6P deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
GN Name=chbG {ECO:0000255|HAMAP-Rule:MF_01246};
GN OrderedLocusNames=KPN78578_12070; ORFNames=KPN_01235;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the degradation of chitin. ChbG is essential for
CC growth on the acetylated chitooligosaccharides chitobiose and
CC chitotriose but is dispensable for growth on cellobiose and chitosan
CC dimer, the deacetylated form of chitobiose. Deacetylation of
CC chitobiose-6-P and chitotriose-6-P is necessary for both the activation
CC of the chb promoter by the regulatory protein ChbR and the hydrolysis
CC of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF.
CC Catalyzes the removal of only one acetyl group from chitobiose-6-P to
CC yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate
CC of ChbF. {ECO:0000255|HAMAP-Rule:MF_01246}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,N'-diacetylchitobiose = acetate + N-acetyl-beta-D-
CC glucosaminyl-(1->4)-D-glucosamine; Xref=Rhea:RHEA:27469,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28681, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:59910; EC=3.5.1.105; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01246};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diacetylchitobiose-6'-phosphate + H2O = acetate + N'-
CC monoacetylchitobiose-6'-phosphate; Xref=Rhea:RHEA:35083,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:64883,
CC ChEBI:CHEBI:71315; Evidence={ECO:0000255|HAMAP-Rule:MF_01246};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01246};
CC -!- PATHWAY: Glycan degradation; chitin degradation. {ECO:0000255|HAMAP-
CC Rule:MF_01246}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01246}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01246}.
CC -!- SIMILARITY: Belongs to the YdjC deacetylase family. ChbG subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01246}.
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DR EMBL; CP000647; ABR76668.1; -; Genomic_DNA.
DR RefSeq; WP_009486060.1; NC_009648.1.
DR AlphaFoldDB; A6T7U7; -.
DR SMR; A6T7U7; -.
DR STRING; 272620.KPN_01235; -.
DR EnsemblBacteria; ABR76668; ABR76668; KPN_01235.
DR KEGG; kpn:KPN_01235; -.
DR HOGENOM; CLU_064244_4_1_6; -.
DR OMA; EPTHIDS; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000000265; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036311; F:chitin disaccharide deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0052777; P:diacetylchitobiose catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd10803; YdjC_EF3048_like; 1.
DR HAMAP; MF_01246; COD; 1.
DR InterPro; IPR022948; COD_ChbG_bac.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR006879; YdjC-like.
DR PANTHER; PTHR31609; PTHR31609; 1.
DR Pfam; PF04794; YdjC; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Chitin degradation; Cytoplasm; Hydrolase;
KW Magnesium; Metal-binding; Polysaccharide degradation; Reference proteome.
FT CHAIN 1..252
FT /note="Chitooligosaccharide deacetylase"
FT /id="PRO_1000067084"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ SEQUENCE 252 AA; 27685 MW; 3E728EE248274549 CRC64;
MERVLIVNAD DFGLSKGQNY GIIEACRNGV VTSTTALVNG AAIDHAAQLG RSTPELAVGM
HFVLTLGEPL SAMPGLTRDG RLGKWIWQQA EEDSLPLEEI AHELACQYHR FVELFGHEPT
HIDSHHHVHM FAQIYPIVAA FAREKGIALR IDRQVAAQSG LDQQAARSSA GFSSEFYGEA
VSEELFLQTL DASIARGERS LEVMCHPAYV DRIIMGSAYC YPRLDELDVL TAASLKAAVA
DRGYRLGTYR DV