GenomeNet

Database: UniProt
Entry: A0A2N7X1Y9_9BURK
LinkDB: A0A2N7X1Y9_9BURK
Original site: A0A2N7X1Y9_9BURK 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system