ID A0A437MW77_9SPHI Unreviewed; 1114 AA.
AC A0A437MW77;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=Glycosyltransferase {ECO:0000313|EMBL:RVU01866.1};
GN ORFNames=EOD41_07875 {ECO:0000313|EMBL:RVU01866.1};
OS Mucilaginibacter limnophilus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1932778 {ECO:0000313|EMBL:RVU01866.1, ECO:0000313|Proteomes:UP000282759};
RN [1] {ECO:0000313|EMBL:RVU01866.1, ECO:0000313|Proteomes:UP000282759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YBJ-36 {ECO:0000313|EMBL:RVU01866.1,
RC ECO:0000313|Proteomes:UP000282759};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVU01866.1}.
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DR EMBL; SACK01000002; RVU01866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437MW77; -.
DR OrthoDB; 9766299at2; -.
DR Proteomes; UP000282759; 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 Reference proteome {ECO:0000313|Proteomes:UP000282759};
KW Transferase {ECO:0000313|EMBL:RVU01866.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1021
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1041..1060
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..412
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 486..675
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 1114 AA; 126953 MW; 57DE8E937D9A2BC7 CRC64;
MSGKQVFQAD TPNRWKRFKW FSRIFFLILI SGLIAAAVTV TDNRYPVLPN LNPSPKKLTK
EQLEQLKRST KFRDFKIQKV QIQKLQEARR QQMLKHAVGK RGINAAFYRA WEPQAYTSLA
DNYQKLDMIV CEGFFIKPGS YTVNTAIDTG IINLNKKYKK QVIVSLSNYV NYNNVSGGFD
TETTRKIIAS AELRKGFINS IVIQLKKYRF NGINLDMYEL DHNDPNFIAF QKELYATLHA
NKLLATHNVI ADDEQYNVEQ LQKYNDYLFL MAIDQHNQSS NEGDVSHQDW VEIILDNVCS
KVPSEKVILV VAGGGYDWPK NSVGVPVGYQ QAISVAKENN SKIIFDPASA NLHYRYTGTD
SLEHNVYFAD AATNFNLMRM ADDWGTAGVA VWRLGFEDPR IWTFIHHNLT IDSLKENGFD
TKKMATVGLN NKIDYIGDGE VLDLITRPHP GKITIKLDTS DYSIIDQNYV ELPTKYVIRR
YGYAPKKVVL TFDDGPDPNY TPRILDILKE ENVPATFFVV GSMVEKNIPI LKRIYDEGYE
IGNHTYLHPD ISQVSLQRVN LELNATRKLI ESITGRSTIL FRPPFNADAE PQTIAEVIPV
EESRKQSYIN IGESIDPWDW QPGVTADSIY ERTIRLADKG SMILLHDAGG DTREPTVQAL
PRIIKELKRR GYKFTTIADV LGKSKDELMP VVKDDVNSGL TGGLYDAVVT GYFYFNWFLF
YVFLTAIFLA LARIVLIGLL AIRQFIENKD RQEAIKLEEL PHVSIIVPAY NEEVTAVKTI
NSLLQLDYPD FDIIFVDDGS KDKTFEVVKA AYGEHPLVKI FTKPNGGKAS ALNYGINHTE
SEFVVCIDAD TQLKNDAIYH LMTCFTDEEI GAVAGTVKVG NEINFITRWQ SIEYITAQNM
DRRAFDLINS ITVVPGAIGA FRKSAINAAG GFTYDTLAED CDLTMRILKQ GYVVRNCGDA
IAYTEAPETV NALLKQRFRW SFGVIQSFWK NKDALFNKKY KFFGMVGMPN ILIFQIILPL
FSPIADLMMI ISLFGPHPER LLNYYLVFLL VDFIVSMIAF RMEKEDYRKL VYIIPQRFIW
RQLMYFVLFK SIRKALKGEL SSWGTLKRTG NVKL
//