ID J2L5L3_9SPHN Unreviewed; 1104 AA.
AC J2L5L3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=PMI04_02573 {ECO:0000313|EMBL:EJK82666.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK82666.1};
RN [1] {ECO:0000313|EMBL:EJK82666.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK82666.1};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJK82666.1}.
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DR EMBL; AJVL01000058; EJK82666.1; -; Genomic_DNA.
DR RefSeq; WP_007710639.1; NZ_CP124576.1.
DR AlphaFoldDB; J2L5L3; -.
DR STRING; 1144307.PMI04_02573; -.
DR PATRIC; fig|1144307.3.peg.2340; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG1215; Bacteria.
DR eggNOG; COG3858; Bacteria.
DR OrthoDB; 276604at2; -.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 Transferase {ECO:0000313|EMBL:EJK82666.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 690..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 980..1005
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1025..1045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1066..1086
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 456..649
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 1104 AA; 120498 MW; FDD95E7E0171B0B7 CRC64;
MTRPIFFDPT GRRGIWARRA LAALLCAIIA ATIAFATTLI AVPSEGDLAL PLPQPRAAHL
TGMSRLRHDL SKWLPHWPDH KPQARPLNVG FYVPDDETSI ASLRRHVGQL DWVVPALVTV
PGRDPHPHFL DDPRLDQMIA SMGRPPKLMP MVQNIGKQGW NGIDAARLLG NPVASRQLAQ
QLAASVAAHH DAGLVMDFES LPSGALPAYL HFLRQLRTDL PARAKLAVTA PAGEDWPLAR
LSQIADHVIF MAYDQHWQGG TPGPIAAQDW FARSVEDASR RIGRDRIIVA LGSYGYDWHD
GGADALSLDE AWLAAHDSDA PVTFDPASGN AGFAYDEDGH RHQVWMLDAA ATWNELQALR
RLGIQGVALW RLGSEDPGVW PGLTAFRNGG RPDLRQVASR LNTDVEGSGE ILRITATPTD
GSRSIAFGPQ GTILRETYHV LPTPYQVQRT GGAQPKMLAL TFDDGPDATW TPKILAVLEH
FHVPGTFFVI GENALEHPGL LQRIVADGDE IGNHSYSHPN LATWSDESTR LELNATQRLV
QAYTGRSMRL FRAPYFGDAE PTTADELGPA LAAQKAGYTV VGLHVDPNDW QRPGTDAIVR
QVIDQVHAAD ADRSGNIILL HDGGGERSQT VAALPQIITT LQKEGYRFVP VSQLAGLSPR
AAMPPVRAGD LTAVRVDVAM FITLAAISAL LGWIFYVAIS LGIARALLMT FLAWFQTRRD
RPAPPVYQPT VSVIIPAYNE ARVIEASVRR VLASDYPALQ LIVADDGSKD ETSAIVARAF
ADDPRVTLLT LQNGGKAAAL NRALKDATGE ILIALDADTQ FEPLTIARLA RWFADPAIGA
VAGDARVGNR VNLVTRWQAL EYITAQNLER RALAGFDAMT VVPGAVGAWR RAALDAVGGY
PEDTLAEDQD LTIAIQRAGW RVTFDPEAVA WTEAPESFKA LSKQRYRWAF GTLQCLWKHA
AILRSRKPTG LALVGMPQAW LFQIVFAAIS PLIDLALILS IAGTILRVQQ HGWAQTNGDV
ATMALYWLVF TGIDIACGWM AYRLDGNKAR YPAHLLVGQR FVYRQIMYWV VVRAIASAIG
GWVVGWGKLE RSGRVSVAPR THQA
//
