ID   CHBG_SALPC              Reviewed;         252 AA.
AC   C0Q659;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
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}; OrderedLocusNames=SPC_2413;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN46525.1; -; Genomic_DNA.
DR   RefSeq; WP_000442734.1; NC_012125.1.
DR   AlphaFoldDB; C0Q659; -.
DR   SMR; C0Q659; -.
DR   EnsemblBacteria; ACN46525; ACN46525; SPC_2413.
DR   KEGG; sei:SPC_2413; -.
DR   HOGENOM; CLU_064244_4_1_6; -.
DR   OMA; EPTHIDS; -.
DR   UniPathway; UPA00349; -.
DR   Proteomes; UP000001599; 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.
FT   CHAIN           1..252
FT                   /note="Chitooligosaccharide deacetylase"
FT                   /id="PRO_1000165049"
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;  28057 MW;  B751EF791109E081 CRC64;
     MERVLIVNAD DFGLSKGQNY GIVEAYRNGV VTSTTALVNG EAIDHAAQLS RELPALGVGM
     HFVLTLGKPV SEMPGLTRDG LLGKWIWQMA EEDTLPLDEI AHELACQYQR FIDVFGREPT
     HLDSHHHVHM FPQIFPIVAR FAAQRGIALR IDRQTVLNAD DLPSDLRSTQ GFSSEFYGEE
     ITEACFLRIL DASTHRGEAS LEVMCHPAFV DNIIRQSAYC YPRLTELEVL TSASLKAAIA
     ERGYRPGSFL DI