ID   CHBG_ECOLI              Reviewed;         249 AA.
AC   P37794; P77435;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Chitooligosaccharide deacetylase ChbG {ECO:0000303|PubMed:22797760};
DE            Short=COD {ECO:0000303|PubMed:22797760};
DE            EC=3.5.1.105 {ECO:0000269|PubMed:22797760};
DE   AltName: Full=Chitin disaccharide deacetylase {ECO:0000303|PubMed:22797760};
DE   AltName: Full=Chitobiose deacetylase {ECO:0000303|PubMed:22797760};
DE   AltName: Full=Chitobiose-6P deacetylase {ECO:0000303|PubMed:22797760};
DE   AltName: Full=Chitotriose deacetylase {ECO:0000303|PubMed:22797760};
DE   AltName: Full=Chitotriose-6P deacetylase {ECO:0000303|PubMed:22797760};
GN   Name=chbG {ECO:0000303|PubMed:9405618}; Synonyms=ydjC;
GN   OrderedLocusNames=b1733, JW1722;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / DH1 / ATCC 33849 / DSM 4235 / NCIB 12045;
RX   PubMed=8121401; DOI=10.1007/bf00281796;
RA   Guzzo A., Dubow M.S.;
RT   "A luxAB transcriptional fusion to the cryptic celF gene of Escherichia
RT   coli displays increased luminescence in the presence of nickel.";
RL   Mol. Gen. Genet. 242:455-460(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
RC   STRAIN=K12;
RX   PubMed=2179047; DOI=10.1093/genetics/124.3.455;
RA   Parker L.L., Hall B.G.;
RT   "Characterization and nucleotide sequence of the cryptic cel operon of
RT   Escherichia coli K12.";
RL   Genetics 124:455-471(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 207-249.
RC   STRAIN=K12;
RX   PubMed=1987146; DOI=10.1128/jb.173.2.514-520.1991;
RA   von Ossowski I., Mulvey M.R., Leco P.A., Borys A., Loewen P.C.;
RT   "Nucleotide sequence of Escherichia coli katE, which encodes catalase
RT   HPII.";
RL   J. Bacteriol. 173:514-520(1991).
RN   [7]
RP   INDUCTION, PATHWAY, AND GENE NAME.
RX   PubMed=9405618; DOI=10.1073/pnas.94.26.14367;
RA   Keyhani N.O., Roseman S.;
RT   "Wild-type Escherichia coli grows on the chitin disaccharide, N,N'-
RT   diacetylchitobiose, by expressing the cel operon.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14367-14371(1997).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-11; HIS-61 AND HIS-125,
RP   DISRUPTION PHENOTYPE, SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=22797760; DOI=10.1128/jb.00533-12;
RA   Verma S.C., Mahadevan S.;
RT   "The chbG gene of the chitobiose (chb) operon of Escherichia coli encodes a
RT   chitooligosaccharide deacetylase.";
RL   J. Bacteriol. 194:4959-4971(2012).
CC   -!- FUNCTION: ChbG is essential for growth on the acetylated
CC       chitooligosaccharides chitobiose and chitotriose but is dispensable for
CC       growth on cellobiose and chitosan dimer, the deacetylated form of
CC       chitobiose. Deacetylation of chitobiose-6-P and chitotriose-6-P is
CC       necessary for both the activation of the chb promoter by the regulatory
CC       protein ChbR and the hydrolysis of phosphorylated beta-glucosides by
CC       the phospho-beta-glucosidase ChbF. Catalyzes the removal of only one
CC       acetyl group from chitobiose-6-P to yield monoacetylchitobiose-6-P, the
CC       inducer of ChbR and the substrate of ChbF. It can also use chitobiose
CC       and chitotriose as substrates. {ECO:0000269|PubMed:22797760}.
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;
CC         Evidence={ECO:0000269|PubMed:22797760};
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:0000269|PubMed:22797760};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q53WD3};
CC   -!- PATHWAY: Glycan degradation; chitin degradation.
CC       {ECO:0000305|PubMed:9405618}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01246}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22797760}.
CC   -!- INDUCTION: By N,N'-diacetylchitobiose. {ECO:0000269|PubMed:9405618}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC       chitobiose and chitotriose. {ECO:0000269|PubMed:22797760}.
CC   -!- SIMILARITY: Belongs to the YdjC deacetylase family. ChbG subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally characterized as part of a cryptic cel operon
CC       for a cellobiose degradation system (PubMed:8121401, PubMed:2179047).
CC       The Cel+ phenotype is due to mutations making expression chitobiose-
CC       independent and altering the substrate specificity. {ECO:0000305}.
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DR   EMBL; X66725; CAA47260.1; -; Genomic_DNA.
DR   EMBL; X66725; CAA47261.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74803.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15514.1; -; Genomic_DNA.
DR   EMBL; X52890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M55161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; E64932; E64932.
DR   RefSeq; NP_416247.1; NC_000913.3.
DR   RefSeq; WP_000440471.1; NZ_SSZK01000001.1.
DR   AlphaFoldDB; P37794; -.
DR   SMR; P37794; -.
DR   BioGRID; 4260305; 16.
DR   IntAct; P37794; 4.
DR   STRING; 511145.b1733; -.
DR   jPOST; P37794; -.
DR   PaxDb; 511145-b1733; -.
DR   EnsemblBacteria; AAC74803; AAC74803; b1733.
DR   GeneID; 946231; -.
DR   KEGG; ecj:JW1722; -.
DR   KEGG; eco:b1733; -.
DR   PATRIC; fig|1411691.4.peg.523; -.
DR   EchoBASE; EB2115; -.
DR   eggNOG; COG3394; Bacteria.
DR   HOGENOM; CLU_064244_4_1_6; -.
DR   InParanoid; P37794; -.
DR   OMA; DHIDSHH; -.
DR   OrthoDB; 9774177at2; -.
DR   PhylomeDB; P37794; -.
DR   BioCyc; EcoCyc:EG12198-MONOMER; -.
DR   BioCyc; MetaCyc:EG12198-MONOMER; -.
DR   BRENDA; 3.5.1.105; 2026.
DR   UniPathway; UPA00349; -.
DR   PRO; PR:P37794; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; 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:0019213; F:deacetylase activity; IMP:EcoCyc.
DR   GO; GO:0052773; F:diacetylchitobiose deacetylase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd10803; YdjC_EF3048_like; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 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:SF1; CARBOHYDRATE DEACETYLASE; 1.
DR   PANTHER; PTHR31609; YDJC DEACETYLASE FAMILY MEMBER; 1.
DR   Pfam; PF04794; YdjC; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Cytoplasm; Hydrolase;
KW   Magnesium; Metal-binding; Polysaccharide degradation; Reference proteome.
FT   CHAIN           1..249
FT                   /note="Chitooligosaccharide deacetylase ChbG"
FT                   /id="PRO_0000051589"
FT   BINDING         61
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q53WD3"
FT   BINDING         125
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q53WD3"
FT   MUTAGEN         11
FT                   /note="D->A: Unable to induce CnbR and to grow on
FT                   chitobiose."
FT                   /evidence="ECO:0000269|PubMed:22797760"
FT   MUTAGEN         61
FT                   /note="H->A: Unable to induce CnbR and to grow on
FT                   chitobiose."
FT                   /evidence="ECO:0000269|PubMed:22797760"
FT   MUTAGEN         125
FT                   /note="H->A: Unable to induce CnbR and to grow on
FT                   chitobiose."
FT                   /evidence="ECO:0000269|PubMed:22797760"
FT   CONFLICT        6
FT                   /note="I -> L (in Ref. 1; CAA47260 and 5; X52890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16..40
FT                   /note="KGQNYGIIEACRNGIVTSTTALVNG -> QRTELRHYRGLSQWDCHCRRRHC
FT                   EW (in Ref. 1; CAA47260 and 5; X52890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="Q -> H (in Ref. 1; CAA47260 and 5; X52890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="R -> C (in Ref. 1; CAA47260 and 5; X52890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="S -> I (in Ref. 1; CAA47260 and 5; X52890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="T -> I (in Ref. 1; CAA47260 and 5; X52890)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  27774 MW;  1D4747904C974F11 CRC64;
     MERLLIVNAD DFGLSKGQNY GIIEACRNGI VTSTTALVNG QAIDHAVQLS RDEPSLAIGM
     HFVLTMGKPL TAMPGLTRDG VLGKWIWQLA EEDALPLEEI TQELVSQYLR FIELFGRKPT
     HLDSHHHVHM FPQIFPIVAR FAAEQGIALR ADRQMAFDLP VNLRTTQGFS SAFYGEEISE
     SLFLQVLDDA GHRGDRSLEV MCHPAFIDNT IRQSAYCFPR LTELDVLTSA SLKGAIAQRG
     YRLGSYRDV
//