ID A0A1Y2Q9W3_9SPHN Unreviewed; 1122 AA.
AC A0A1Y2Q9W3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=CAP40_17335 {ECO:0000313|EMBL:OSZ64412.1};
OS Sphingomonas sp. IBVSS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1985172 {ECO:0000313|EMBL:OSZ64412.1, ECO:0000313|Proteomes:UP000194216};
RN [1] {ECO:0000313|EMBL:OSZ64412.1, ECO:0000313|Proteomes:UP000194216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVSS2 {ECO:0000313|EMBL:OSZ64412.1,
RC ECO:0000313|Proteomes:UP000194216};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-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:OSZ64412.1}.
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DR EMBL; NFUR01000005; OSZ64412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2Q9W3; -.
DR STRING; 1985172.CAP40_17335; -.
DR OrthoDB; 276604at2; -.
DR Proteomes; UP000194216; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000194216};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 695..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 975..1008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1028..1047
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..393
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 458..651
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 1100..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 122820 MW; 1F94E7C1BB8C21FD CRC64;
MERPIFFDAS GKRNRWTMRA FFALLLVIVL AAGAFAMTVV RVPTPGPLAM ALEHPQPRSL
KQQANRLRHS FASWLPQGPA KASAAPLAVG FYVPWDDASG ASLRRHINEL DWVVPSLYTV
TGPQHHIATA PDTEFDPILA SATRRPKVLP MVQNATGDNW DSTGAAALLR DPKTRAAFLD
ELQRALVARK ADGAVFDFEE LPTASQRDYL ALLREARARF AAAKMSIAVT VPAQDDDWNM
KAYAAAADHV ILMNYDEHAP ATAAGPIASQ AWFVRQMNAA LTQVPAQKLI VGIANYGYNW
TAPGKADPIS IEEAWLIAHD SEATVTFDKA SGNQSFAYEE NGIEHTVWMA DATTAWNQLR
AANIKGVGGV ALWRLGSEDS NFWAALGAAH SGKIPDLRRI EAVGDVDVEG SGEILRITST
PSVGARTIVQ NPQGLIVDEI FQSLPTPYVV TRTGYMPGKV ALTFDDGPDA DWTPKILDVL
KQKQVTGTFF MIGENAMAEP FLVRRVVDEG HEIGSHTFTH PNLALTSSRG TRIELNATQR
LIEAYTGRSV RLFRAPYFGD AEPTTADELI PALTAQRAGY TNVGLHVDPN DWQRPGVDAI
VDTTLREVEA GNAEQSGQII LLHDGGGDRS QTLAALPRII DGLRAKGYQF VPVSQLAGLS
RDQVMPEVQE GDLAAVRMDV GIFLVAATLG FMLKWSFFLA IALGIARALV LAGLAVNGNR
RKNRPVAPEI VPDRFVSVLI PAYNEAKVIE ASIRRVLASE QVNVEVIVLD DGSQDGTGDL
VRAAFADEPR VKLLTLENGG KARALNHGLA LARGDIVIAL DADTQFEPLT IARLARWFED
PEVGAIAGNA KVGNRINLVT RWQAVEYVTS QNLERRALAS LDAIMVVPGA VGAWRKAALE
DVGGYPIDTL AEDQDLTIAI QRKGWRVGYD IDAVAWTEAP ESFRALAKQR FRWAFGTLQC
LWKHRAILRT RKPAGLALVG IPQAWVFQIA FALISPLIDL ALIASIVGTA IRVWQHGWAQ
TESDVLRMGI YWISFMAIDF LCGWVAYRME KREKRYPGLL LLAQRFVYRQ LMYWVVIRAV
ANALRGPWVG WGKLERSGRV EAQATPETQA AQETRETQAT AA
//