ID B4W4T5_9CYAN Unreviewed; 883 AA.
AC B4W4T5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=MC7420_1555 {ECO:0000313|EMBL:EDX70811.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX70811.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX70811.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX70811.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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 -!- 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}.
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DR EMBL; DS989881; EDX70811.1; -; Genomic_DNA.
DR RefSeq; WP_006106382.1; NZ_DS989881.1.
DR AlphaFoldDB; B4W4T5; -.
DR STRING; 118168.MC7420_1555; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_011907_1_0_3; -.
DR OrthoDB; 9766299at2; -.
DR Proteomes; UP000003835; 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; 2.40.10.220; 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 Glycosyltransferase {ECO:0000313|EMBL:EDX70811.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003835};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDX70811.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 51..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 554..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..357
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 609..705
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 883 AA; 100973 MW; EE99465BA4DA64AB CRC64;
MTSPSSKSKS KLSRTRFWIS PQKREQLTHW LVDHLPHAFD QFFQWLSNNQ ILLLIGSLVL
LLHPLITARP AIWQQALVTA LLLAVGRLAL QMEGQKPTKK KSEYIHLFLV LLSLVTTVRY
LYYRVNYTLN LDDWLNGIFS LLLFVAELYA ILTLVLAYFQ TLKIKDRQPV DLSLYPEEQW
PKVDIYIPTY NEDVEIVRKT TLCALAIDYP ADKKKVYVLD DGRAEKYKAR RAELRKTCEE
LGAIMLTRDN NDHAKAGNIN TAFRRTTGDL VLILDCDHMP VKQFLKHTVG FFFDPQVAFV
QTPHWFFNPD PFERNLLTKG KIPVGNELFY KVLQKGNDFW NAAFFCGSAA VIRKEYALQI
GGIATETVTE DCHTAFRLHS LGYKSFYYDK IMVAGLAPEK FSAYVGQQVR WARGMAQILR
LENPLINPKL NLTIPQRICY FSATSHFFYG YPRMMYALAP PLFLLFGINS VKGLGLETLC
YALPHIILSM QTNHIPYKHV RFSFWNEIFE FAMSFQAGIV TLLAVVNPGL GSFNVTDKGL
SVTKRSFDFE SVRYLVIVSA IASASLLTLP FWLILSPEDT QAVLINALWC IFNLFLLLAA
VLVAFEQPQL RRAHRLQRKL TAIIHSGGSS WTGETIDVSE TGAQILLDEW PNIPDEVKIE
LVGDYGARVL LNARVLRAMA TSKLQAKIFV DFISLSRTQI DDLTLVIFSD VKEWFSQSRV
EEDNPWESLK FIVTSIKRVF VEFRPAIAEK MGVKSTVRKQ VQAVAQLYWD GWEGHSYTAR
VMEIGTQDLR LEFDEHHILN LETMQQTRPL IGLLVSQEKN APQPQSLLAQ VEMIEELVPT
PTGGRLEQVT NAPTYRIAME LSFPESLKRQ QQPKIQRLLK TLE
//
