ID A0A255YR65_9PROT Unreviewed; 254 AA.
AC A0A255YR65;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=CHU95_21425 {ECO:0000313|EMBL:OYQ31699.1};
OS Niveispirillum lacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Niveispirillum.
OX NCBI_TaxID=1981099 {ECO:0000313|EMBL:OYQ31699.1, ECO:0000313|Proteomes:UP000216998};
RN [1] {ECO:0000313|EMBL:OYQ31699.1, ECO:0000313|Proteomes:UP000216998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH1-14 {ECO:0000313|Proteomes:UP000216998};
RA Cai H.;
RT "Niveispirillum cyanobacteriorum sp. nov., isolated from cyanobacterial
RT aggregates in a eutrophic lake.";
RL Submitted (JUL-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYQ31699.1}.
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DR EMBL; NOXU01000032; OYQ31699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255YR65; -.
DR Proteomes; UP000216998; Unassembled WGS sequence.
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; cd10917; CE4_NodB_like_6s_7s; 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; 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:UP000216998};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..254
FT /note="Chitooligosaccharide deacetylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012084246"
FT DOMAIN 68..248
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 254 AA; 26634 MW; 505F41861747DAAB CRC64;
MRGEEMGLLH YGAKCALIMS AVLLSMPVLA ADCGPDALGT SRTLLLKRGT GGAFGSLQHA
ALPGLAPGEV VLTFDDGPVP ALTPQVLDAL KAECAKATFF MTGSNLDTHG EIAKRVTEEG
HSAGIHSYSH PQLGTLSAAA QLDDLSHTQA AYQRVFGVPA PSYRFPFLGE TPVLMAALAK
DGVTVFSIDL GITDWQPADT TAILADRLSK ALDEKGGGII LMHDANPPTA AAIPTLLRVI
KQKGYRLVHV AWEG
//
