ID A0A248JU44_9PROT Unreviewed; 341 AA.
AC A0A248JU44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=Y958_13075 {ECO:0000313|EMBL:ASG21628.1};
OS Nitrospirillum amazonense CBAmc.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1441467 {ECO:0000313|EMBL:ASG21628.1, ECO:0000313|Proteomes:UP000197153};
RN [1] {ECO:0000313|EMBL:ASG21628.1, ECO:0000313|Proteomes:UP000197153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBAmC {ECO:0000313|EMBL:ASG21628.1,
RC ECO:0000313|Proteomes:UP000197153};
RA Schwab S., dos Santos Teixeira K.R., Simoes Araujo J.L., Soares Vidal M.,
RA Borges de Freitas H.R., Rivello Crivelaro A.L., Bueno de Camargo Nunes A.,
RA dos Santos C.M., Palmeira da Silva Rosa D., da Silva Padilha D.,
RA da Silva E., Araujo Terra L., Soares Mendes V., Farinelli L.,
RA Magalhaes Cruz L., Baldani J.I.;
RT "Complete genome sequence of Nitrospirillum amazonense strain CBAmC, an
RT endophytic nitrogen-fixing and plant growth-promoting bacterium, isolated
RT from sugarcane.";
RL Submitted (JUN-2017) 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 -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000256|ARBA:ARBA00010973}.
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DR EMBL; CP022110; ASG21628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248JU44; -.
DR KEGG; nao:Y958_13075; -.
DR Proteomes; UP000197153; Chromosome 1.
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; IPR006311; TAT_signal.
DR PANTHER; PTHR43123; POLYSACCHARIDE DEACETYLASE-RELATED; 1.
DR PANTHER; PTHR43123:SF1; POLYSACCHARIDE DEACETYLASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Reference proteome {ECO:0000313|Proteomes:UP000197153}.
FT DOMAIN 101..319
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 37..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 37793 MW; 0C84F3063543A3AE CRC64;
MTTDITASRR SFLTHAGAGA GLLAAGMAMG GAAAGAAETK TPATKPTAAK SQETKSQGGF
WPGDTRLVIS VSMQFEAGGQ PLKGTDSPFP KVDFPDSVPS DAVANTWFAY GYREGVPRML
DLWDKHGVKV TSHMIGEAVR KNPNLAREIV KRGHEAAGHG PRWSSEYAMS REEERQFLTD
ARTMVAEVTG QTPVGYNANW LRRGPYTLPL LQELGYLYHI DDVSRDEPFI EQVNGHDFVV
VPYTLRNNDI VLIEGRNYTP TQFLEQVTLD FDQLYEEAGH RRRMMSISAH DRISGTPQMV
RVWDKFLTYA KSHPGVTFLR KDEIARFAAG SPLTVRETET I
//
