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CHBG_ECO24
ID   CHBG_ECO24              Reviewed;         252 AA.
AC   A7ZMK0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=EcE24377A_1954;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV18368.1; -; Genomic_DNA.
DR   RefSeq; WP_000440445.1; NC_009801.1.
DR   AlphaFoldDB; A7ZMK0; -.
DR   SMR; A7ZMK0; -.
DR   EnsemblBacteria; ABV18368; ABV18368; EcE24377A_1954.
DR   KEGG; ecw:EcE24377A_1954; -.
DR   HOGENOM; CLU_064244_4_1_6; -.
DR   OMA; EPTHIDS; -.
DR   UniPathway; UPA00349; -.
DR   Proteomes; UP000001122; 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; 2.
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.
FT   CHAIN           1..252
FT                   /note="Chitooligosaccharide deacetylase"
FT                   /id="PRO_1000067078"
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;  28014 MW;  9BB5ECE26B6636CB CRC64;
     MERLLIVNAD DFGLSKGQNY GIIEACRNGI VTSTTALVNG QAIDHAVQLS RDEPSLAIGM
     HFVLTMGKPL TAMPGLTRDG VLGKWIWQLA EEDALPLEEI TQELASQYLR FIELFGRKPT
     HLDSHHHVHM FPQIFPIVAR FAAEEGIALR IDRQPLSNAG DLPANLRSSQ GFSSAFYGEE
     ISEALFLQVL DDASHRGDRS LEVMCHPAFI DNTIRQSAYC FPRLTELEVL TSASLKYAIA
     ERGYRLGSYL NV
 
 
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