ID A0A2N7X1Y9_9BURK Unreviewed; 722 AA.
AC A0A2N7X1Y9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-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 Name=bcsA {ECO:0000313|EMBL:PMS35591.1};
GN ORFNames=C0Z20_16965 {ECO:0000313|EMBL:PMS35591.1};
OS Trinickia symbiotica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=863227 {ECO:0000313|EMBL:PMS35591.1, ECO:0000313|Proteomes:UP000235777};
RN [1] {ECO:0000313|EMBL:PMS35591.1, ECO:0000313|Proteomes:UP000235777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPY 581 {ECO:0000313|EMBL:PMS35591.1,
RC ECO:0000313|Proteomes:UP000235777};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
RL Submitted (JAN-2018) 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|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|RuleBase:RU365020}. 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:PMS35591.1}.
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DR EMBL; PNYC01000010; PMS35591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7X1Y9; -.
DR STRING; 863227.GCA_000373005_00611; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000235777; 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 InterPro; IPR003919; Cell_synth_A.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
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; PF13632; Glyco_trans_2_3; 1.
DR PRINTS; PR01439; CELLSNTHASEA.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU365020};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365020};
KW Reference proteome {ECO:0000313|Proteomes:UP000235777};
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 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 50..66
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 73..92
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 420..441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 527..549
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 555..579
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT DOMAIN 247..433
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
SQ SEQUENCE 722 AA; 79901 MW; AFBB8FE739085A05 CRC64;
MLVLIADWIS SDQYARKSQM LPNVYKLTAV LSLAGLAALA ILSVGLPHPI ANACGLLAVF
AILVPVQTPL TRPLLLAFSG FLITRYIAWR FASFPIGGGL PTELVAAALL AAELYCMGVS
LLSYFVSARP LERRPLPLPD DPRALPFVDV YIPTYSEPLS VVAPTVCGAV EIDYPKERFR
VFVLDDGFPR ARTAQRAEQR RELAERAERL KALAARHGAV YLTRESNAHA KSGNLNTAMR
STSGDLIAIL DADHVPTRDF LRATVGFFLA DPKIALVQTP HFFTNPDPVE KNLGLFSRTP
AENDLFYRVV QKGLDTWNAS FCCGSGAVVR RAAMEEIDGF STDSITEDAS TSVKLHQRGW
HSAYLSRPMV AGLQPETISG FLVQRIRWGV GMMQILMKQN PWFVRGLSLT QRVAYSSVGL
FWFFPFARLV TFAVPIVSIV FKLQTYPGGA NNLVGYTLPY LVSAVLTAER LNGRFRRIFS
SELYETIQAF YVLPALVSAL LRPNSPIFQV TPKGEKSDID FISEFRLPFY AIFVGSLVGL
IWGGVRLALE PESRAILVAA VAWIGFNLFL SFGALGALFE KAQRRVRPRI VMGDPVTLVG
PFGEREALLV DANEIGLRIR LHEPLSLERF ALRFGNRLLN ARVISAADSA RGEYVGLYTP
QSAEEERAAV VLAYGDSERW LRQWKQREAR ANFLRSFIGM LALSAKGAHA HARHVGRKVF
HG
//