ID A0A0A2VYQ5_BEABA Unreviewed; 1004 AA.
AC A0A0A2VYQ5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming] {ECO:0000256|RuleBase:RU365020};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU365020};
GN ORFNames=BBAD15_g1220 {ECO:0000313|EMBL:KGQ13031.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ13031.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ13031.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ13031.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes
CC uridine 5'-diphosphate glucose to cellulose.
CC {ECO:0000256|RuleBase:RU365020}.
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 -!- 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:KGQ13031.1}.
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DR EMBL; ANFO01000064; KGQ13031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VYQ5; -.
DR STRING; 1245745.A0A0A2VYQ5; -.
DR HOGENOM; CLU_011907_5_0_1; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000030106; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR InterPro; IPR003919; Cell_synth_A.
DR InterPro; IPR017746; Cellulose_synthase_operon_BcsQ.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009875; PilZ_domain.
DR NCBIfam; TIGR03030; CelA; 1.
DR NCBIfam; TIGR03371; cellulose_yhjQ; 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; PF06564; CBP_BcsQ; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF141371; PilZ domain-like; 1.
PE 4: Predicted;
KW c-di-GMP {ECO:0000256|RuleBase:RU365020};
KW Cell inner membrane {ECO:0000256|RuleBase:RU365020};
KW Cell membrane {ECO:0000256|RuleBase:RU365020};
KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916,
KW ECO:0000256|RuleBase:RU365020};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU365020};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365020};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
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 284..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 308..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 362..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 687..709
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 799..824
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT DOMAIN 411..580
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 828..924
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 1004 AA; 114330 MW; 1F8561308CDBE9DC CRC64;
MQDEETGNAQ ENKLVYAFQN DFLALKPKGW ARAMLDNEDW RKSAWRYTSH LDVLPFGQLS
PAERETFDTV EKALGQFSHF LADLKASQQY QWILLDLPHG FSALTRQILA QTDSVVTVVK
PDTNCHIRLH QQALPKGAHI LVNYLLVASQ LQDDIYQVWL QSQRTMIPIV LHRDEAMAES
AAVKQPLGEY RPDSLIAEEI MTLANWSLPR PLDVVRYGIQ SLWLLLRASG QAGRPRIRSF
GRIQAWRESW HGWLEKLPEN FSHRTQHLDQ KKELSHISHT ARRILLGVIV AFSAILALLC
ITQPFNPLSQ FIFLMLLWGV ALLVRRLPGR FAALMLIVLS LTVSCRYIWW RYTSTLNWND
PLSLAFGLGL LFAETYAWLV LVMGYFQVVW PLNRQPVPMP KDMNTWPVVD IFVPTYNEEL
HVVKGTIYAS LGIDWPKDKL NIWILDDGGR DEFKQFADMV GVNYIARPTH EHAKAGNINN
ALKYAKGDFV AIFDCDHVPT RSFLQLTMGW FFKEKSLAMM QTPHHFFSPD PFERNLGRFR
KTPNEGTLFY GLVQDGNDMW DATFFCGSCA VIRRGPLDEI GGIAVETVTE DAHTSLRLHR
RGYTSAYLRI PQAAGLATES LSAHIGQRIR WARGMTQIFR LDNPFFGKGL KFAQRLCYAN
AMFHFLSGIP RLIFLTAPLA FLLFHAYIIY APAIMIALFV LPHMIHASLT NSKIQGKYRH
SFWSEIYETV LAWYIAQPTL VALFNPHKGK FNVTAKGGLV ENEYVDWVIT RPYLVLVLIN
LLGVAFGAWR FFYGPENEAL TVLVSLLWVF YNLIILGGAV AVSVESKQVR RAHRVEIAMP
AALAREDGHL FPCTVHDYSD GGVGIKIHGP TQVLEGQKVN LLLKRGAQEF YFPAQVVRVF
GDEVGLQLAQ MTTKQHIDFI QCTFARADTW ALWQDSFPED KPLESLVDIL KLGFRGYRHL
AEFAPPSLKF VFHAITVLVD WIVSFIPHSP TTEPAKRRTL SALA
//
