ID K9WQQ8_9CYAN Unreviewed; 919 AA.
AC K9WQQ8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=Mic7113_6521 {ECO:0000313|EMBL:AFZ22099.1};
OS Allocoleopsis franciscana PCC 7113.
OG Plasmid pMIC7113.02 {ECO:0000313|EMBL:AFZ22099.1,
OG ECO:0000313|Proteomes:UP000010471}.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ22099.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ22099.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ22099.1,
RC ECO:0000313|Proteomes:UP000010471};
RC PLASMID=pMIC7113.02 {ECO:0000313|EMBL:AFZ22099.1,
RC ECO:0000313|Proteomes:UP000010471};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished plasmid 2 of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-2012) 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; CP003632; AFZ22099.1; -; Genomic_DNA.
DR RefSeq; WP_015211493.1; NC_019760.1.
DR AlphaFoldDB; K9WQQ8; -.
DR KEGG; mic:Mic7113_6521; -.
DR PATRIC; fig|1173027.3.peg.7214; -.
DR HOGENOM; CLU_011907_1_0_3; -.
DR Proteomes; UP000010471; Plasmid pMIC7113.02.
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; PF13632; Glyco_trans_2_3; 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 Plasmid {ECO:0000313|EMBL:AFZ22099.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFZ22099.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..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..526
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 271..463
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT DOMAIN 609..703
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 919 AA; 104404 MW; 719B95C0CCE3A362 CRC64;
MTSTSSKVRE KPSRKHIGIS NEQRKRLSNL LVERVPQAFD AVLQALPHTH LLVLIGSLIW
LSIPIIAVRP AIWQQGVVAA VLIAVGRIVL QMEEQQPTKK VSEYLHLFLI VVSVVTTLRY
LYYRVNYTLN FDDIINGFFC FLLFTAELYA ICTLVLAYFQ TLKIKDRKPI DLSLYPQEQW
PKVDIYIPTY NEDVEIVRKT TLCALAIDYP ADKKQVYVLD DGRAEKYKAR RAELRQMCEE
LGATMLVRDN NEHAKAGNIN TAFKVTKGDL VLILDCDHMP VKDFLMHVVG FFFNPKVAFV
QTPHWFYNPD PFERNLLTQG KIPVGNELFY KVLQKGNDFW NAAFFCGSAA VIRKEYALQI
GGIATETVTE DCHTAFRLHS LGYESVYYDK IMVAGLAPEK FSAYVGQQVR WARGMAQILR
IENPLINRKL NLTIPQRICY FSATSHFFYG FPRLMYAIAP PLFLLFGINS VKGLGLETLF
YALPHIILSM QTNHIPYKHV RFSFWNEIFE FAMSFQAGIV TLLALVNPKL GSFNVTDKGL
SVTKRSFDFD SVRYLVIVGA IGAASLLAVP FWLWLSPEDT QAVLINTFWC IFNLSLVLAA
ILVAFEQPQL RRAHRLPRKL TAIIHEGNQS WQGTTVDVSE SGCQVLLDEW PNIPDEVKIE
LVGDFGARAL LSGKVIRAIA TSKLQARLFI DFVEPTRTQI DDLTLVIYCD VKEWYSQTRT
EVDDPIESLK FIITSIKRVF REFRPAIGVK VRKQVNGFAH LYWEGWEGHS YTATLTEIGT
QDVRLEIDGS DIFNLEEMQS TQPVIGLLLS QEENDSQPTS LLAKVELIEP LSNPSFGNSS
PAKAKMLEVA TPRSVELETA IQENTTLQER VADKNSAKLR HRSGTKSENT NLYAIELSFP
ESLKRQQQAK IKRLLTTLN
//
