ID R0EJ38_CAUVI Unreviewed; 1120 AA.
AC R0EJ38;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
DE Flags: Precursor;
GN ORFNames=OR37_02053 {ECO:0000313|EMBL:ENZ82009.1};
OS Caulobacter vibrioides OR37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ82009.1, ECO:0000313|Proteomes:UP000013063};
RN [1] {ECO:0000313|EMBL:ENZ82009.1, ECO:0000313|Proteomes:UP000013063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR37 {ECO:0000313|EMBL:ENZ82009.1,
RC ECO:0000313|Proteomes:UP000013063};
RX PubMed=23792749;
RA Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA Palumbo A.V., Brown S.D.;
RT "Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
RT Tolerant to Heavy Metals.";
RL Genome Announc. 1:0-0(2013).
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:ENZ82009.1}.
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DR EMBL; APMP01000010; ENZ82009.1; -; Genomic_DNA.
DR RefSeq; WP_004619229.1; NZ_APMP01000010.1.
DR AlphaFoldDB; R0EJ38; -.
DR STRING; 1292034.OR37_02053; -.
DR PATRIC; fig|1292034.3.peg.2039; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG1215; Bacteria.
DR eggNOG; COG3858; Bacteria.
DR OrthoDB; 276604at2; -.
DR Proteomes; UP000013063; 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: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 CDD; cd06549; GH18_trifunctional; 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; IPR001223; Glyco_hydro18_cat.
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; PF00704; Glyco_hydro_18; 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; PS51910; GH18_2; 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:ENZ82009.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 22..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1039..1062
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..409
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 473..665
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 1120 AA; 122689 MW; 5853826BDBE8E453 CRC64;
MTPDDRHIFH DPTGKRERRA KLVLGVFISA VAAIVAGFVA TLAFAPRLPD APLKDPHVLT
SLHQETPRKT KVAKTWRHVP RPKDETTATG AKALSVGFYV PWDEDSRESL RRNVDKLDVI
SPQWIAINGS GGDINIVDDP EGAARIANAP KPPAVLPLVH NSANAAFNGP MGDALLVNPA
ARAKLIATLK DLAAQRGYGG YVFDFEALGP KGLAAYPKFL EEARAAFAGT DREVWVTAPF
DEEGWPLKRL EQASDTLVLM AYDQHYALGD PGPNAGQDWY ERELAQRFAS LDPNRSVLAL
GAYGYDWTLK KDGTRASGAP ATFHEAMRNA QDAGATIRMD PETLNPTYSY TDDNGDNHVV
WFLDAVTLFN QIKVTDAWKP RGYGLWRMGM EDPGVWTLLG KPYGQISASG LTTLANGQGV
DFDGGGEVLR VASLPTPGKR SMEFDHQTGL ISGESYDVIP SSYVIERYGQ KKGLVALTFD
DGPDGRWTPK ILDILKAKHA PATFFVIGQN MQRRPDLVQR EVAEGHNVGG HSWTHPNIAE
TPLPQVQVEL NATQRLFEVL TGRSMRLFRP PFFGDAEPST PHEVAPLVIA QTLGYMTVGL
RIDTDDWQKP SPQQIIDRAL DRLDNPGNRP GQVVLLHDAG GDRSHTVQAL PGLIDAIRAR
GYRLVTIGEL AGLTPEQTMP KTSRTALDLA LDRLGFDFFR GFQKIMTGLF ITAIFLGVAR
LVFLASLALV HRFWTHDEPA DLDPDNGPLV SVLIPCFNEE KVIAASVARI LESKWKNLEV
LVLDDGSKDR TADEVRAHFA NDPRVTLLSF ENGGKARAVN RGLAVAKGEY VVALDADTLF
PPETIGRLAR WFQDEDIGAV AGNAIVGNRV NVVTRWQALE YVTAQNLERR ALAALGAVTV
VPGAVGAWRK SVLDALGGYP ADTLAEDQDL TIACQRAGWK VAFDPDARAY TEAPDTVGGL
LKQRFRWSFG TLQCVWKHRK AMFNTKTPVL GFVALPQIWL FQIILAVAAP LVDLGVVWSL
ISSVYAAVAH PVEWRPDDLI LGLIYWAVFI GVDLSAGALG MILEKRAPWS DLPFLPVQRF
GYRQLMYYVV VKSVVMAIRG GRVGWGKLER RGSVSVKAGG
//
