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Database: UniProt
Entry: H7C7W0_BRADU
LinkDB: H7C7W0_BRADU
Original site: H7C7W0_BRADU 
ID   H7C7W0_BRADU            Unreviewed;       219 AA.
AC   H7C7W0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   Name=nodB {ECO:0000313|EMBL:BAC47291.1};
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC47291.1, ECO:0000313|Proteomes:UP000002526};
RN   [1] {ECO:0000313|Proteomes:UP000002526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC   {ECO:0000313|Proteomes:UP000002526};
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC47291.1; -; Genomic_DNA.
DR   RefSeq; NP_768666.1; NC_004463.1.
DR   RefSeq; WP_011084823.1; NZ_CP011360.1.
DR   AlphaFoldDB; H7C7W0; -.
DR   STRING; 224911.AAV28_06965; -.
DR   EnsemblBacteria; BAC47291; BAC47291; BAC47291.
DR   GeneID; 83557202; -.
DR   KEGG; bja:blr2026; -.
DR   PATRIC; fig|224911.44.peg.1528; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_021264_0_1_5; -.
DR   InParanoid; H7C7W0; -.
DR   OrthoDB; 9784220at2; -.
DR   PhylomeDB; H7C7W0; -.
DR   Proteomes; UP000002526; Chromosome.
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   InterPro; IPR026402; Nodulat_NodB.
DR   NCBIfam; TIGR04243; nodulat_NodB; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT   DOMAIN          21..213
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   219 AA;  23962 MW;  2BE06EBFA26CD06A CRC64;
     MTERSTLSTV RCDYADAGGS RAVHLTFDDG PNPFCTPEVL DVLAQHRVPA TFFVIGTYAT
     EHPELIRRMI AEGHEVANHT MTHPDLSRCG PTELHDEVLT ASEAIRLACP LASPRHMRAP
     YGIWTRDVLA VAASAGLTAL HWSVDPRDWS RPGVDAIVNS VLANVRPGAI VLLHDGYPPD
     EEGLPSGSTL RDQTRTALAY LIPALQRRGF VIRPLPQLH
//
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