ID   NODB_RHILP              Reviewed;         229 AA.
AC   P24150;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Chitooligosaccharide deacetylase;
DE            EC=3.5.1.-;
DE   AltName: Full=Nodulation protein B;
GN   Name=nodB;
OS   Rhizobium leguminosarum bv. phaseoli.
OG   Plasmid sym p42d.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE-3;
RX   PubMed=1991718; DOI=10.1128/jb.173.3.1250-1258.1991;
RA   Vazquez M.V., Davalos A., Las Penas A., Sanchez F., Quinto C.;
RT   "Novel organization of the common nodulation genes in Rhizobium
RT   leguminosarum bv. phaseoli strains.";
RL   J. Bacteriol. 173:1250-1258(1991).
CC   -!- FUNCTION: Is involved in generating a small heat-stable compound (Nod),
CC       an acylated oligomer of N-acetylglucosamine, that stimulates mitosis in
CC       various plant protoplasts.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Plasmid p42d was originally thought to originate from
CC       Rhizobium leguminosarum (biovar phaseoli). {ECO:0000305}.
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DR   EMBL; M58626; AAA98210.1; -; Genomic_DNA.
DR   PIR; D38180; D38180.
DR   AlphaFoldDB; P24150; -.
DR   SMR; P24150; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR026402; Nodulat_NodB.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   TIGRFAMs; TIGR04243; nodulat_NodB; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nodulation; Plasmid.
FT   CHAIN           1..229
FT                   /note="Chitooligosaccharide deacetylase"
FT                   /id="PRO_0000172752"
FT   DOMAIN          21..214
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT   ACT_SITE        28
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   SITE            149
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   229 AA;  25061 MW;  F7A292EF9735D3CF CRC64;
     MTAPALLCEV HGERDDGTGR PSLYLTFDDG PHPFCTPEIL DILAEHRVPA TFFVIGEFLA
     DQSKLIQRMI AEGHHEVANH TMTHPDLSDC EPRRVQRQIL ETNRAIKMAS PGGGAAHPRA
     PYGIWTEEVL KASANAATHA VHWSVDPRDW SSPGADAIVN DVLQSVRPGA IVLLHDGCPP
     DEMQQGADHS LRHQTIMALS SIIPALHDRP LCIYTLRLLG SSEDPMDIA