ID Q8DHZ8_THEVB Unreviewed; 722 AA. AC Q8DHZ8; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539}; DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539}; GN OrderedLocusNames=tlr1795 {ECO:0000313|EMBL:BAC09347.1}; OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1). OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales; OC Thermosynechococcaceae; Thermosynechococcus. OX NCBI_TaxID=197221 {ECO:0000313|EMBL:BAC09347.1, ECO:0000313|Proteomes:UP000000440}; RN [1] {ECO:0000313|EMBL:BAC09347.1, ECO:0000313|Proteomes:UP000000440} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IAM M-273 / NIES-2133 / BP-1 RC {ECO:0000313|Proteomes:UP000000440}; RX PubMed=12240834; DOI=10.1093/dnares/9.4.123; RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the thermophilic cyanobacterium RT Thermosynechococcus elongatus BP-1."; RL DNA Res. 9:123-130(2002). CC -!- CATALYTIC ACTIVITY: CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)- CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA- CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12; CC Evidence={ECO:0000256|ARBA:ARBA00000122}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004429}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000039; BAC09347.1; -; Genomic_DNA. DR RefSeq; NP_682585.1; NC_004113.1. DR RefSeq; WP_011057632.1; NC_004113.1. DR AlphaFoldDB; Q8DHZ8; -. DR STRING; 197221.gene:10748400; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; BAC09347; BAC09347; BAC09347. DR KEGG; tel:tlr1795; -. DR PATRIC; fig|197221.4.peg.1877; -. DR eggNOG; COG1215; Bacteria. DR Proteomes; UP000000440; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro. DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro. DR CDD; cd06421; CESA_CelA_like; 1. DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1. DR InterPro; IPR003919; Cell_synth_A. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR009875; PilZ_domain. 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; PF00535; Glycos_transf_2; 1. DR Pfam; PF07238; PilZ; 1. DR PRINTS; PR01439; CELLSNTHASEA. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF141371; PilZ domain-like; 1. PE 4: Predicted; KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000440}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 12..28 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 54..72 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 81..98 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 118..141 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 387..404 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 416..438 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 450..468 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 480..498 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 519..540 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 560..580 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 167..334 FT /note="Glycosyltransferase 2-like" FT /evidence="ECO:0000259|Pfam:PF00535" FT DOMAIN 582..688 FT /note="PilZ" FT /evidence="ECO:0000259|Pfam:PF07238" SQ SEQUENCE 722 AA; 82314 MW; 729D85646681A869 CRC64; MRLKSLPTDG WLLLLGILAL LGILLWQLDW RNLLPNLVGF WHEGQAIMRP QGTTLEALLL PAFVWLAITF LLKELSPKPT FWSRLIVSVG IALLGIRYEL WRFFGSLNLD DRLNGTISLA LFLAELLTVL NSVAFFFHCI FSIDRTPEAD RLSQAVIRGE YLPWVDVILP TYNEGVEILR RSVIACQAMD YPHKRIYLLD DTRRPAVRAL AKELGCEYRD RPDNRHAKAG NINHALPTLT GELIAVFDAD FMPTRNFLTR TVGFFQDAKT AMVQTPQHFF NEDPVTVNLG LEGIVNNEQT LFFRFIQPSR DFFNAVVCCG TCFVIRRSAL DEIGGIPTDS ITEDYMTTIK LQTRGYRVKY LNEALAAGMS PETISAYINQ RLRWGQGTLQ MLFLGGNFLT APNLRLTQRL SHALSIIYWF LSIPRVIFLL APLAFLLFGI APLRATVNEI LYFYFPYYLG NIMAFSWLTE GRRSAFWSDV YETIIAFPMA ITVIRTLISP RGKTFKVTPK GVVDPHRINI NWPLIRPLMI IAILTIGGLI WRSSPLQETI VNPDSLAVNV VWSIYNLSLL LVCMLVAIDV PQRRHPRFLR SEPCELIVGG DRYRGQTVDI SEEGVRIRLN RFPPESLGQS VGELHFLEPS PFINLRLPVQ VRWSRTANLG SKSLVLEIGV QFLSLSIAQQ RHLINYLYCQ PGQWDEVRVP EVKTTWALLQ SIFRLYPLAE SR //