ID A0A226I0A3_9FLAO Unreviewed; 1131 AA.
AC A0A226I0A3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Glycosyl transferase family 2 {ECO:0000313|EMBL:OXA99802.1};
GN ORFNames=B0A75_09775 {ECO:0000313|EMBL:OXA99802.1};
OS Flavobacterium oncorhynchi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=728056 {ECO:0000313|EMBL:OXA99802.1, ECO:0000313|Proteomes:UP000198336};
RN [1] {ECO:0000313|EMBL:OXA99802.1, ECO:0000313|Proteomes:UP000198336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 59446 {ECO:0000313|EMBL:OXA99802.1,
RC ECO:0000313|Proteomes:UP000198336};
RA Stine C., Li C., Tadesse D.;
RT "Whole genomes of Flavobacteriaceae.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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:OXA99802.1}.
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DR EMBL; MUHA01000012; OXA99802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226I0A3; -.
DR Proteomes; UP000198336; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR001173; Glyco_trans_2-like.
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; PF00535; Glycos_transf_2; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:OXA99802.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1057..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..417
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 492..683
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 1131 AA; 129291 MW; FA0F36F6117ADFFA CRC64;
MDGKKQVFQT VTQKRWKTFQ WSSRLILFIL ILMVPIFFIT LKRGLKPPLP LLANSSRAGH
SLENPVTPKN LTDKELKKFK GFDYFLRAKN KIDKLKKQPA VAKTASEVRA AFYVDWDPQS
LFSLQKNIDK LNMVIPEWFF IDPKTDLLRT EIDTAALKVM KKGKVKILPL INNINESLGE
GEFDGDLIHR ILHDTNKRER LINDIVKALK KYDLQGINID FEEFKENADE PIIAFQKSLY
EKLHPLGYLV TQDIMANDED FNIKALSKYN DYMFLMAYDE HYAGSIPGEI SSQKWIERIV
DKTAKEIPSD KIILCFAGYG YDWQEKQEGQ TITYDQAIAV AKQYNATIKF DNNSYNNSFK
YADSNGKKHE VNFEDAATNF NTIRFSDEYG LAGTALWRLG SEDQRLWTYY HRSLTNESLK
NKPFDFKVMK RVNTRIESPA YIGDGEILNV IADPAPGKIE LEIDKEETII TEQRYVELPT
KYVISKFGNV NKQVILTFDD GPDPIYTPEI LDILKREKVP AVFFVIGIQG ENNIPLLQRI
YKEGHEIGNH TFTHPNIALV SPERAAKEME TTRLLIEAVT GRSTVLFRAP YNADAEPTTE
AELKPIALSK AQNYYTVGES IDPNDWEKGV SADSIYKRTI SQYEANPDKG IILLHDAGGN
REATVAALPR IIKYFKDRNI QFTTVSHLLG KTKEEIMPEA KGPFISLDNF IFDFGYWFGH
FITATFWVAI FMGFLRIALM AVMAFIKKWK DHKYPPVYKD FEGELPKVSI IVPAYNEEIN
AVKTIENLLG QDYPFFDIVF VDDGSKDKTF AMINEAFANN PKVKVHTKPN GGKASALNYG
IALTQNDYVI CIDADTQLKT DAVSQLMKGF RIQLKNNEEI GAIAGNVKVG NENTMLTKWQ
SIEYTTAQNF DRRAFDLING ITVVPGAIGA FKKEAIEKAG GFTTDTLAED CDLTIRILRN
DYHIINCIEA VAVTEAPESL KEFMKQRFRW SYGIMQAFWK NREACFNPRY KGLGMVALPN
ILLFQIVLPI FAPLADLVLI LSLFWNYNDP DSLHKILIYY IAFMLVDMLV SVIAFIFEKE
KLTKLIWLIP QRFVYRQLMY VILFKALRRA IKGESQSWGV LTRTGNVATV K
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