ID A0A0M3AVP9_9SPHN Unreviewed; 1114 AA.
AC A0A0M3AVP9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=YP76_04550 {ECO:0000313|EMBL:KKW93920.1};
OS Sphingobium chungbukense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW93920.1, ECO:0000313|Proteomes:UP000033874};
RN [1] {ECO:0000313|EMBL:KKW93920.1, ECO:0000313|Proteomes:UP000033874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ77 {ECO:0000313|EMBL:KKW93920.1,
RC ECO:0000313|Proteomes:UP000033874};
RA Kim Y.-C., Chae J.-C.;
RT "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT chungbukense DJ77.";
RL Submitted (APR-2015) 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:KKW93920.1}.
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DR EMBL; LBIC01000001; KKW93920.1; -; Genomic_DNA.
DR RefSeq; WP_046762355.1; NZ_LBIC01000001.1.
DR AlphaFoldDB; A0A0M3AVP9; -.
DR STRING; 56193.YP76_04550; -.
DR PATRIC; fig|56193.3.peg.935; -.
DR Proteomes; UP000033874; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10962; CE4_GT2-like; 1.
DR CDD; cd06423; CESA_like; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43630; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR PANTHER; PTHR43630:SF1; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR Pfam; PF13641; Glyco_tranf_2_3; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 683..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 997..1013
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1025..1047
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1067..1089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..654
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 1114 AA; 122157 MW; FA43FE4591C6A210 CRC64;
MSRPIFFDPT GRRGLWARRI LAGGLLAILL AAIAFATTLV AVPTERDLAL PLPQPHAARL
SGISTLRRDI AKWLPHWGKT HGQAKPLNIG FYVPGTENSI ASLRRHVGQL DWVVPALVNV
AGPAQPIHYA SDPVFDRMIA AMPRPPKVLP MVQNLGTESW NGAGAARVLR DPVASRALAQ
QLAAYVARRH EAGLVMDFES LPGSAMPTYL HFLHLLRAQL PAGAKLAVTV PVDEEGWPLA
RFADVTDRVI LMAYDQHWQS GQPGPIAAQD WFTRQVKTAL RDIGADHIVV ALGSYAYDWH
GTGDGGTADA LSLDEAWLAA HDSDAPPIYD MASGNAGFAY DEAGQRHQIW MLDAAATWNE
LLVLKRLGIQ SMALWRLGSE DPGVWADLTA WRNGGRPNLS RMASTLNTDV EGAGEILRIT
ATPTEGRRTI VFGPQNSIER ESYGTLPTPY QVQRTGGQHP KMLALTFDDG PDPTWTPKIL
KVLERMHAPA TFFVIGENAL EHPGLLQRIV ADGDEIGNHT YDHPNLATWS DDATRLQLNA
TQRLVQAYTG HGMRLFRAPY FGDAEPTTAD ELGPALAAQR LGYTVVGLHV DPNDWQRPGT
DAIVSQVMDQ VHDVSDDRSE NIILLHDGGG DRAQTVEALP RIITQLRAEG YSFVPVSQLA
GLPRQAAMPP VKSSDLLAVR VDVGVFVVLA VLSALLGWIF YLAISLGLAR AVLMTLLAWF
QERRERIVPP EHQPTVSVII PAYNEARVIE ASVRRVLASD YPALQLIVAD DGSKDETSAI
VERAFADDPR VTLLTLQNGG KAAALNRALA QAHGEIVIAL DADTQFEPQT IRRLARWFAD
PAIGAVAGDA RVGNRVNLVT RWQAVEYITA QNLERRALAG FDAMTVVPGA VGAWRRAALD
AVGGYPENTL AEDQDLTIAI QRAGWRVTYD PEAVAWTEAP ESFKALAKQR YRWAFGTLQC
LWKHRRILRE RRPTGLALVG MPQAWLFQIL FAAISPLIDF ALITSIVGTI VRVHQHGWAQ
TSNDVWMMGL YWLAFTGIDI ACGWVAYRLD DRDIGYPPHL LVAQRFVYRQ IMYWVVVRAI
ASAIGGWVVG WGKLERSGRV AVAAQDKPLI PSGA
//
