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Database: UniProt
Entry: Q70ZW4_9BRAD
LinkDB: Q70ZW4_9BRAD
Original site: Q70ZW4_9BRAD 
ID   Q70ZW4_9BRAD            Unreviewed;       152 AA.
AC   Q70ZW4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
DE   Flags: Fragment;
GN   Name=nodB {ECO:0000313|EMBL:CAD23471.1};
OS   Bradyrhizobium sp. ORS 88.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=186890 {ECO:0000313|EMBL:CAD23471.1};
RN   [1] {ECO:0000313|EMBL:CAD23471.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ORS88 {ECO:0000313|EMBL:CAD23471.1};
RX   PubMed=15012950; DOI=10.1016/S1055-7903(03)00255-0;
RA   Moulin L., Bena G., Boivin-Masson C., Stepkowski T.;
RT   "Phylogenetic analyses of symbiotic nodulation genes support vertical and
RT   lateral gene co-transfer within the Bradyrhizobium genus.";
RL   Mol. Phylogenet. Evol. 30:720-732(2004).
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. {ECO:0000256|ARBA:ARBA00003236}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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DR   EMBL; AJ430716; CAD23471.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q70ZW4; -.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Nodulation {ECO:0000256|ARBA:ARBA00022458}.
FT   DOMAIN          21..152
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   NON_TER         152
FT                   /evidence="ECO:0000313|EMBL:CAD23471.1"
SQ   SEQUENCE   152 AA;  16714 MW;  12C5E752DA1CF35B CRC64;
     MKRHDCLSVV RSEYPDIDGS RSVYLTFDDG PNPLCTPAIL DALAEHQCPA TFFVIGVHAA
     DQPGLVRRMI AEGHEVANHT MTHPDLSRCE PADVEHQIVA TSRLINAACP QASVRHVRAP
     YGRWTDEVLA LSAQSGLAAL HWSVDPLDWS RP
//
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