ID A0A370G3X5_GLULI Unreviewed; 1545 AA.
AC A0A370G3X5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU365020};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU365020};
GN ORFNames=C7453_10627 {ECO:0000313|EMBL:RDI37304.1};
OS Gluconacetobacter liquefaciens (Acetobacter liquefaciens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=89584 {ECO:0000313|EMBL:RDI37304.1, ECO:0000313|Proteomes:UP000254958};
RN [1] {ECO:0000313|EMBL:RDI37304.1, ECO:0000313|Proteomes:UP000254958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5603 {ECO:0000313|EMBL:RDI37304.1,
RC ECO:0000313|Proteomes:UP000254958};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU365020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU365020};
CC -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC {ECO:0000256|RuleBase:RU365020}.
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 -!- SIMILARITY: In the C-terminal section; belongs to the AcsB/BcsB family.
CC {ECO:0000256|ARBA:ARBA00010653}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 2 family. {ECO:0000256|ARBA:ARBA00010003}.
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:RDI37304.1}.
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DR EMBL; QQAW01000006; RDI37304.1; -; Genomic_DNA.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000254958; Unassembled WGS sequence.
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 c-di-GMP {ECO:0000256|RuleBase:RU365020};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|RuleBase:RU365020};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU365020};
KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916,
KW ECO:0000256|RuleBase:RU365020};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU365020};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365020};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365020};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365020};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365020}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 44..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 66..84
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 96..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 400..419
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 425..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 505..528
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 740..759
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 1507..1526
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT DOMAIN 146..315
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 565..664
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
FT REGION 799..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1545 AA; 169798 MW; 493DF6C97EBBFB5C CRC64;
MMRRLDMTVN SGLLRRVALD SAFAAIVGLT LIVLVSALQL SDTQQGLFAL GTVGLLLLVN
RFQGRLASCF LITLSIMMSL RYIVWRVGTT ITHDNILQFT LSIALLLAEC YALWVLCLSY
FQMVWPLGRQ VHPLPEDESL WPSVDVFIPT YHESLDVVRA TVLAAQALDW PADKLNVYLL
DDGRRQAFHD FALESGAGYI TRPDNRYAKA GNLNHALEVT GGALVVVFDC DHVPVHDFLK
QTVGWLVADP TMSILQTAHY FYSADPFQRN LTAVEQVPPE GNMFYGLIQD GNDLWDSTFF
CGSCAVIRRK ALESVGGFAT ETVTEDAHTA LKMQRKGWST GYLRLALAGG LATERLIFHI
GQRMRWARGT LQIIRLDNPL FGSGLRWEQR LCYLSSMSHF LFAIPRIIFL TAPMAFLLLG
QNVLMASPLA ALAYAGPHIV HSMLTLSRIE GRWRYTFWSE LYETSLAMFL VRVTISTFLQ
PTKGSFNVTR KGTQLHNNYF DLRAVYPNVV LAILLGAAVL RGIFGVFIEH LDPAEFQSML
LNTFWGLFSL FMVLASIAVA RETRQSRVQH RVRADLPVHV RMASGEVWKT RTTDLSLGGV
GLLAPGGAQL NGPTQVMLDY YDAQDHINVS VPVEILRQRG DRMHGRWLIS DLDQERQVVS
MIFGRRDAWD SWSDFPRDRP FKSFFIILRN IAAMFRPRSG EVRSSVIPAD DASSDGVATA
QTLEKASFVL KPSRQATQRG VVASCVLVAG LAMAGIPVAH GQTDGTPLGS IPAEGDPTLA
LPMPAPPEAR PAITLPARPS TPGAPGLPID DPNAGDRNPA IGSDAAIATR ISDTEVTNTL
SLHDLGVSGP MILRGYSPLQ GVTVGIPANR IVTHAQLTLS GALSPELLPE ASAVTVTLNE
QYIGTIKVDP AHPQFGPLTF DVNPMYFGGK NTLNFQFAGE YRRDCNDLYN EVLWARISDQ
SHITLTTVRI APERTLARLP APFFDPNLRT PVRVPMVLSA NEPNLRASGM IASWFGKLAD
FRQFSFPVTN AIPDAGNAIQ IGENLPVGPD GQLPQGPTLL EIPNPNDRWG TVLVVTGRNP
REVEVAARTL VLSPTTLGAV NAQVVSDVAT TPRKPYDAPS FVPTDRPVRF GELVPADTLQ
ANGFAPALLN MPFHLPTDLF TWRQRPFLMD LWVHPPGVIG GTSVDLASSR LDVSVNDIFL
QRSSMIASGS WDTWSRRLLN PHFGTVGIQV ALPPETLFGQ NQLQFAFDAR PVDRGACRHV
PIDLHTSVDE SSVLDFRRAY HFTSLPDLAQ FAQIGFPFTR MADLSETTVV MPRHPDNAVI
GAYLDLMGVF GATTWYPTTD VSIAYAGDAD AEPPSGDIIL LTTAGKVHEV DTLLSRSPYQ
VDQSWITVGQ HTALQGIRNL FQDRDQAGLR NAVTAKLRAP IAGAGLLIGA QSPSDPHRSV
VAIIGDTPQR LQEMVLALRD NTVHPMIQGD LVIKNGDQVS SYRTAPRYTV GSLPLWMWPA
WYLDGHLLAL SVIGLLGTGL LAYVIWRALK RRARRRLGDM PSNDD
//
