ID A0A0G0P7I3_9BACT Unreviewed; 887 AA.
AC A0A0G0P7I3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=UT08_C0008G0017 {ECO:0000313|EMBL:KKQ85261.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_38_8.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618570 {ECO:0000313|EMBL:KKQ85261.1, ECO:0000313|Proteomes:UP000034081};
RN [1] {ECO:0000313|EMBL:KKQ85261.1, ECO:0000313|Proteomes:UP000034081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC {ECO:0000256|ARBA:ARBA00007754, ECO:0000256|PROSITE-ProRule:PRU01100}.
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:KKQ85261.1}.
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DR EMBL; LBVL01000008; KKQ85261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0P7I3; -.
DR STRING; 1618570.UT08_C0008G0017; -.
DR Proteomes; UP000034081; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:InterPro.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR000805; Glyco_hydro_26.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43867; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR PANTHER; PTHR43867:SF2; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR Pfam; PF02156; Glyco_hydro_26; 1.
DR Pfam; PF13632; Glyco_trans_2_3; 1.
DR PRINTS; PR00739; GLHYDRLASE26.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51764; GH26; 1.
PE 3: Inferred from homology;
KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU01100};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01100};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKQ85261.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 538..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 570..871
FT /note="GH26"
FT /evidence="ECO:0000259|PROSITE:PS51764"
FT ACT_SITE 703
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT ACT_SITE 813
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ SEQUENCE 887 AA; 102649 MW; 210FC3F224A1A422 CRC64;
MLQDYYQKAS RLKKLFIKAG ILYALILVTF YAVFRAYYIN LTPSLLIFSI LLYIAEMHTV
ILMYGFLYSL WPRKYRSYNR INNNKNLQIN MFVTVCGEPL DVVKETISHA KRAAEKYIRE
VNPKEKPRVI VLNDGKAAKK EGWQDVADYC EDAGVEHVER ETNEGFKAGN INNGLKVYPA
DDPHNTIDCF FDADFCAKEE FLLEILKPLA DDSVDFVQSP QRYKNMNTWV AQGAGAHQIF
FFDYVCPAKA YDNALFLCGT NYAIRREALL QAGGVDNRFV TEDYATSIKL HLMGKRGVFI
SKVLALGMAP MNLKEYFNQQ TRWCKGCLDA NGKYLKELLF GPLNWKQKFH YFLSTVYYFI
GVRDLILILA PIPYLFWGVS LIRANTIQYL AFIYLPLMIF NFSLFFVTFQ NPIKSLVLDV
VSFPVFAKAF LASVIGKNLP FSVTIKKYEK ENPFKVYRNQ LIVALVLISG LIFSTITKSN
YNIHGHLINY FWATYDALFL SIGFILVVRE NYNISFIESK VMAIYRNVLF TLNLSKRIAF
NPAVLGFGAM LIVLFVGRGV IDGTLAYENT VEKVLPQKTN TELLVPGGGI YYGYYLPELD
THPNDPKINV IDGEQPTMVM YYQDWNQNSN FNAKFMQKLW DKNVIPIITW EPWDAQQNSV
APINQNGYPQ KLIPEGYYDS YIREYAKSAK KWNKPFFLRF AHEMNGNWYP WGNIEKESAQ
NYIKMWKHVH NIFNEEGADN VIWVWSPNNT DMYGETEGVL DFYPGYDYVD WVGFSSFNWG
TANEWNQWMD FKSASWKVYS KFLTLNKPIM VSETSSVSQG GDKNNWFWQT LNKDIPSMPM
IRAVIIFNDD FNKADFSLSS GMDEVSIIKN YLIDNGYYLK KLLLSEY
//
