ID   A0A0C9M018_SPHPI        Unreviewed;       288 AA.
AC   A0A0C9M018;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=SP6_11_00140 {ECO:0000313|EMBL:GAN12515.1};
OS   Sphingomonas paucimobilis NBRC 13935.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN12515.1, ECO:0000313|Proteomes:UP000032025};
RN   [1] {ECO:0000313|EMBL:GAN12515.1, ECO:0000313|Proteomes:UP000032025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN12515.1,
RC   ECO:0000313|Proteomes:UP000032025};
RA   Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA   Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL   Submitted (AUG-2014) 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:GAN12515.1}.
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DR   EMBL; BBJS01000011; GAN12515.1; -; Genomic_DNA.
DR   RefSeq; WP_042468529.1; NZ_BBJS01000011.1.
DR   AlphaFoldDB; A0A0C9M018; -.
DR   GeneID; 78526313; -.
DR   Proteomes; UP000032025; 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; cd10941; CE4_PuuE_HpPgdA_like_2; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR045235; CE4_PuuE_HpPgdA-like_2.
DR   InterPro; IPR022560; DUF3473.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR014344; PEP-CTERM_polysacc_deacetyl.
DR   NCBIfam; TIGR03006; pepcterm_polyde; 1.
DR   PANTHER; PTHR47561; POLYSACCHARIDE DEACETYLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G05030); 1.
DR   PANTHER; PTHR47561:SF1; POLYSACCHARIDE DEACETYLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G05030); 1.
DR   Pfam; PF11959; DUF3473; 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}.
FT   DOMAIN          25..288
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   288 AA;  31912 MW;  47042B35A6AE607F CRC64;
     MPPDPGAAAP LNGMSVDVEE WFQVGAFEKT IDKGDWDRLD SRVEANTDAV LSLFAETGTR
     ATFFTLGWVA HRHPGLIRRI VAAGHEMASH GWDHQRVFTM TADQFRADLA RAKAAIENAG
     GQAVTGYRAP SFSIDTRTPW AHPVLAEAGY RYSSSVAPLR HDHYGWAESP RYAWRPLADA
     DLIELPVTVA QWGQRRLATG GGFFRMLPAK LTDIAVGQVN RDRHGAIFYF HPWEVDPDQP
     RVADAPLRSK VRHYSRLGAM AGKLRGLLGR HDWGRVVEVA AEEAARLA
//