ID   A0A2S8BAT6_9SPHN        Unreviewed;       288 AA.
AC   A0A2S8BAT6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=CVO77_00955 {ECO:0000313|EMBL:PQM29521.1};
OS   Sphingopyxis lindanitolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=2054227 {ECO:0000313|EMBL:PQM29521.1, ECO:0000313|Proteomes:UP000238954};
RN   [1] {ECO:0000313|Proteomes:UP000238954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WS5A3p {ECO:0000313|Proteomes:UP000238954};
RA   Kaminski M.A.;
RT   "The complete genome sequence of Sphingopyxis pomeranensis sp. nov. strain
RT   WS5A3p.";
RL   Submitted (NOV-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:PQM29521.1}.
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DR   EMBL; PHFW01000001; PQM29521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8BAT6; -.
DR   OrthoDB; 9787041at2; -.
DR   Proteomes; UP000238954; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238954}.
FT   DOMAIN          54..273
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   288 AA;  33064 MW;  16B9798E78E65C0F CRC64;
     MKEERIDWPN GAKMALSVVV NVEEGSEMTV ARGDRGMEPV DELGIHIKSP IRNYSNESNY
     LYGIKAGAPR VVRLLRDYGI MASWTVAALS LENHPEIAQA IADLGHEPVS HGWRWVHQFK
     MDEAQEREFI RKAAASIEKT VGVRPYGWLS RYFHTDNTRR LLIEEGFTYH MDDYSGDVPF
     WDRDTVPGKP IAIVPYQLDS NDMKMWTDPA MTPVQWLDYA KNCFDQLYRE GEAGNPKMMS
     LGLHLRIIGR PGRIWALEEF FRHVTARKDV WITTRHAIAQ HLAQVDPA
//