ID Q11EC3_CHESB Unreviewed; 257 AA.
AC Q11EC3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=Meso_2876 {ECO:0000313|EMBL:ABG64252.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG64252.1};
RN [1] {ECO:0000313|EMBL:ABG64252.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG64252.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG64252.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11EC3; -.
DR STRING; 266779.Meso_2876; -.
DR KEGG; mes:Meso_2876; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_1109741_0_0_5; -.
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 CDD; cd10967; CE4_GLA_like_6s; 1.
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; PTHR34216; -; 1.
DR PANTHER; PTHR34216:SF11; CHITOOLIGOSACCHARIDE DEACETYLASE; 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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 36..257
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 257 AA; 28394 MW; CDA8E64FDA1F99DF CRC64;
MMGGLGKDTG ELIDRAVNRL LWKMGSRRRE VVTDTPLVTF TFDDVPDTAL SNGAGILERH
DARGTFYIAG GLGSQVEADR TLISREGCRE LSLRGHEIGC HTFAHRKLRN LGGALRADLT
RNEAYLREAG VEQPIRNFAY PFNAAWPPAR RALHARYATC RGAGEAINRG STDHLMLKGV
EIRQPETHAR SLTRWIDDVA AEPGWLVFFT HDIAEVPTPF GCTPGTFEHL VSYAVAKGCR
IVTVGEAVSL LGWENKR
//
