ID A0A1Y6GAR7_9BACI Unreviewed; 1229 AA.
AC A0A1Y6GAR7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase {ECO:0000313|EMBL:SMQ84856.1};
GN ORFNames=SAMN05444673_6125 {ECO:0000313|EMBL:SMQ84856.1};
OS Bacillus sp. OV166.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ84856.1, ECO:0000313|Proteomes:UP000194454};
RN [1] {ECO:0000313|EMBL:SMQ84856.1, ECO:0000313|Proteomes:UP000194454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV166 {ECO:0000313|EMBL:SMQ84856.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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DR EMBL; FXWM01000001; SMQ84856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6GAR7; -.
DR OrthoDB; 9766299at2; -.
DR Proteomes; UP000194454; 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:SMQ84856.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..846
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1120..1139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1145..1166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1187..1207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..533
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 598..785
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 1229 AA; 138899 MW; 1F24FD473BDF675E CRC64;
MNRIFRWIVR SLFAPVTGNA GAVASTLGFF MGFFPLDSFR IPLLLVLSLL LRLNIIALFL
GTLIPLFIPK MNHLPFLDMR LLEDYWLFST LQSKIQLSQT MASGVLGGLI GLVCYFIFHW
FYNLGLKKRE RNQEHVFLDP AKRRWSIIKR MSAGFTVLII LVSTIFIESL NTNPEFPELQ
LNKSAVKSGI EPINKSFSAE QLATQFQKTS PSPLIQKNIG QSNKKQEVYG FYVDWDKNSH
TSFKKNSDSI TTLVPGWMQL TPGLTLKTST DKSIIAEAKA HNIKILPLVN NFSNNKWDGE
ALHRLFITPG AEDLFIKKML EYVRTNDFDG INIDFEDIQP KDKEDFTHFI GKVYEAFHPH
GLMVTLDVPP NNNSFNYTSL ATNVDRMIVM LYDQHHSMSK PGPVAPSDWV KENLNQLHIP
SEKLIVSLGS FGYDWEENSH QPADTVAFGD IMDLGIGTNL QIQWNKQIGN PYVRYKRNGK
NHVVWFLDAA SFYNQMKLVI DHGSRGIAVW RLGSEDPSIW NFLNKPKGIT DPSHALQTLV
SPKSVHYTGA GEILKIASPS EKGTRTIQLD SHGLIQTETY TKLPKPSEVV RYGQPKGKEV
VLTFDDGPDP TYTPQILDIL DKNHIKGSFF IIGENALQHP ELVNKMYKKG HEIGNHTFTH
PDVASITPFQ TRMELNANQR LFQEITGHSM TLFRPPYVAN AEPSTKSELE PILRAQDMGY
TMVGELIDSD DWQRLSSDEI VNRVLDQLPE GNVILMHDAG GDRSNTVEAL PTIIKELKQR
GYTFTTIADL TGKSDSQIMP PVKDSPYLVY DKAVFMVIQG WHLGLSFLFY SAILLGILRL
AIFVFLSRKQ VKRYKETVID PNFTPFVSVV IAAYNEEKVI CKTVDSILSS DYPAFEILII
DDGSKDDTAV VVQETYTKHP LVRLIKKNNG GKSSAVNLGF KEANGEIVVA LDADTLIAEN
AISLLVNHFK NENVAAVSGN VKVGNKGNLL TNWQHIEYVT GFNLERRAFA ALNCITVVPG
AIGAWRKTAV EDAGYFQEDT LAEDTDITLT LLRQGKKIEF EEKAYAFTEV PEDIKSLAKQ
RYRWVYGTLQ CLWKHRDALF NKKHNSLGFI ALPNMWLFQY IYQTISPIAD ILFILALFNP
HPERAAIGFI LFYLLDFGTS LYAFRLEKES PKPLASLFLQ RILYKQLMTY VVIKSIFSAI
KGVTVGWGKL KRKGNVTQET SMVKVKENM
//
