ID BCSA5_KOMXY Reviewed; 1518 AA. AC Q9WX75; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-SEP-2023, entry version 93. DE RecName: Full=Putative cellulose synthase 3; DE Includes: DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming]; DE EC=2.4.1.12; DE Includes: DE RecName: Full=Cyclic di-GMP-binding domain; DE AltName: Full=Cellulose synthase 3 regulatory subunit; GN Name=bcsABII-B; OS Komagataeibacter xylinus (Gluconacetobacter xylinus). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=28448; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=JCM 7664 / NBRC 13693; RX PubMed=10382968; DOI=10.1093/dnares/6.2.109; RA Umeda Y., Hirano A., Ishibashi M., Akiyama H., Onizuka T., Ikeuchi M., RA Inoue Y.; RT "Cloning of cellulose synthase genes from Acetobacter xylinum JCM 7664: RT implication of a novel set of cellulose synthase genes."; RL DNA Res. 6:109-115(1999). 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 -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- DOMAIN: There are two conserved domains in the globular part of the CC catalytic subunit: the N-terminal domain (domain A) contains the CC conserved DXD motif and is possibly involved in catalysis and substrate CC binding. The C-terminal domain (domain B) contains the QXXRW motif and CC is present only in processive glycosyl transferases. It could be CC involved in the processivity function of the enzyme, possibly required CC for holding the growing glycan chain in the active site. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC glycosyltransferase 2 family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the AcsB/BcsB family. CC {ECO:0000305}. 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; AB015804; BAA77600.1; -; Genomic_DNA. DR AlphaFoldDB; Q9WX75; -. DR SMR; Q9WX75; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR UniPathway; UPA00694; -. 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; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1. DR InterPro; IPR003919; Cell_synth_A. DR InterPro; IPR003920; Cell_synth_B. DR InterPro; IPR018513; Cell_synthase_bac. DR InterPro; IPR005150; Cellulose_synth. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR009875; PilZ_domain. DR NCBIfam; TIGR03030; CelA; 1. 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; PF03170; BcsB; 1. DR Pfam; PF03552; Cellulose_synt; 1. DR Pfam; PF00535; Glycos_transf_2; 1. DR Pfam; PF07238; PilZ; 1. DR PRINTS; PR01440; CELLSNTHASEB. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF141371; PilZ domain-like; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Cellulose biosynthesis; KW Glycosyltransferase; Membrane; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..1518 FT /note="Putative cellulose synthase 3" FT /id="PRO_0000059266" FT TRANSMEM 24..44 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 71..91 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 105..125 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 404..424 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 428..448 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 465..485 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 514..534 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 543..563 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1481..1501 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 569..668 FT /note="PilZ" FT REGION 1..731 FT /note="Catalytic" FT REGION 144..237 FT /note="Catalytic subdomain A" FT REGION 314..374 FT /note="Catalytic subdomain B" FT REGION 732..1518 FT /note="Cyclic di-GMP binding domain" FT /evidence="ECO:0000250" FT REGION 765..785 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 767..781 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 186 FT /evidence="ECO:0000255" FT ACT_SITE 330 FT /evidence="ECO:0000255" FT SITE 233 FT /note="Important for substrate binding" FT /evidence="ECO:0000255" FT SITE 235 FT /note="Important for substrate binding" FT /evidence="ECO:0000255" SQ SEQUENCE 1518 AA; 166465 MW; 7D7634503183DAB6 CRC64; MYGTWFTTGK VTDLLARTGL DRVPVWVPVV LGVVLMAFVG SVRIDPALQG WVSIGTVTLL LVLNRRRGRG ITVFLMMLSL LVSLRYIVWR LTATVQFSNW LQTALAVLLL LAEAYALMTL CLSYFQMAWP LRRREHPLPE DMAQWPSVDV FVPSYNEELS LVRSTVLGAL DLDWPADRLN VYILDDGRRK AFHDFAVEAG AGYIIRAENN HAKAGNLNHA LAVTDSPFAV IFDCDHVPTR GFLRRTIGWM MADPNLALLQ TPHHFYAPDP FQRNLAGGMH VPPEGNMFYG LVQDGNDFWD ATFFCGSCAI IRREAVMGIG GFATETVTED AHTALKMQRR GWGTAYLREP LAAGLATERL ILHIGQRVRW ARGMIQIMRL DNPMLGAGLR WEQRLCYLSA MSHFLFAIPR LTFLVSPLAF LFLGQNIIAA SPLAISVYAL PHIFHSVITL SRIEGRWRYS FWSEIYETSL ALFLVRITIV TLLQPHKGKF NVTDKGGLLA RGYFDWDAVY PNVILAGVLC AALLRGVFGI VWQFHDRLAL QSFILNTLWV VISLIIVLAS IAVGRETRQT RNAPRVSVRL PVVVTDAHGR QMEGHTHDIS LGGLAVGTRL ATPDMVGGEV TVRYDSARDG IHVGVPARVL DARDGTLRLR WAVRDLEDER QVVSMVFGRN DAWAGWADFA PDRPLRSLAM VFRSIGGLLR RRPAEAPRAL HEMGEGELPA TEEKLEKQSF VLKPVPRSAR HGATASAALF VAFTALVPAA MAQEAPSPDQ SGVTAETPFG DSNTGVVPDA LPAIDPAVAD RISDAEVTRT LTFRNLGATT GPLTLRGYSP LQGLDVVVPA NRVVTHAQLT LSGALSPSLL PEANAVTVTL NEQYVGTLKV DPQHPQFGPV SFDIDPLYFT GDNKLNFHFA GEYRRDCNDL FNEILWARIS DMSRITLTTV RITPERKLSR LPAPFFDPNQ RSTLRVPVVL PATGDRGALR AAGLVASWFG RIADFRKLSF PVSTTIPASG NAVEVGVNLP VDAEGGRPAG PMLAEVANPN DRWGTVLVVT GRTAQEVEVA ARALVFSPDT LGGVASKVVS DVSLETRHPY DAPAFVPTDR PVRFGELVGA ADLQGGGFAP AGMTLPFHLP PDLYTWRGRP FLMNMWVRAP GGPVVDLETS RVDVSLNNNY LQSYTLSPPG LWRKWSERLV NQHAGAVGHV TALPPWLLFG QNQLQFNFDA RPIDRGACRR TPGDIHMSVD SDSTLDFRRG YHFAEMPNLS YFAEAAFPFS RMADLSETTV VLPDHPDTGT TGAFLDLMGF FGASTWYPAA GVTVMGADEV AQTPPKGDIV VLGTAAQLGG AASGLLARSP YVIHDRHITV GQRMGLQGIW YLFQDHDHAG LKDGVTANLN APIAEAGVLL AAQSPYDSQR SVVAFTGDTP ERIHDLVLSL RNKGDLPSLQ GDLVLKNGDR FTSYRTAPVY TVGSLPLWLR LDWFLGHHPS ALYLAGLAGA GLAALGVWAW LRGWSRRRIA RDDLTGEL //