(data stored in ACNUC29543 zone)

SWISSPROT: B2JS37_PARP8

ID   B2JS37_PARP8            Unreviewed;       743 AA.
AC   B2JS37;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Cellulose synthase catalytic subunit [UDP-forming] {ECO:0000256|RuleBase:RU365020};
DE            EC=2.4.1.12 {ECO:0000256|RuleBase:RU365020};
GN   OrderedLocusNames=Bphy_3256 {ECO:0000313|EMBL:ACC72414.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72414.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose =
CC         [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP;
CC         Xref=Rhea:RHEA:19929, Rhea:RHEA-COMP:10033, Rhea:RHEA-
CC         COMP:10034, ChEBI:CHEBI:15378, ChEBI:CHEBI:18246,
CC         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}.
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DR   EMBL; CP001044; ACC72414.1; -; Genomic_DNA.
DR   RefSeq; WP_012402587.1; NC_010623.1.
DR   STRING; 391038.Bphy_3256; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ACC72414; ACC72414; Bphy_3256.
DR   GeneID; 27742945; -.
DR   KEGG; bph:Bphy_3256; -.
DR   eggNOG; ENOG4107QZ7; Bacteria.
DR   eggNOG; COG1215; LUCA.
DR   HOGENOM; HOG000259144; -.
DR   KO; K00694; -.
DR   OMA; QRLCYAN; -.
DR   OrthoDB; 724641at2; -.
DR   BioCyc; BPHY391038:G1GBS-3353-MONOMER; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000001192; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Gene3D; 3.90.550.10; -; 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   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF07238; PilZ; 1.
DR   PRINTS; PR01439; CELLSNTHASEA.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03030; CelA; 1.
PE   4: Predicted;
DR   PRODOM; B2JS37.
DR   SWISS-2DPAGE; B2JS37.
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|RuleBase:RU365020};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU365020,
KW   ECO:0000313|EMBL:ACC72414.1};
KW   Membrane {ECO:0000256|RuleBase:RU365020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW   Transferase {ECO:0000256|RuleBase:RU365020,
KW   ECO:0000313|EMBL:ACC72414.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU365020};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU365020}.
FT   TRANSMEM     40     56       Helical. {ECO:0000256|RuleBase:RU365020}.
FT   TRANSMEM     86    104       Helical. {ECO:0000256|RuleBase:RU365020}.
FT   TRANSMEM    119    141       Helical. {ECO:0000256|RuleBase:RU365020}.
FT   TRANSMEM    411    430       Helical. {ECO:0000256|RuleBase:RU365020}.
FT   TRANSMEM    436    460       Helical. {ECO:0000256|RuleBase:RU365020}.
FT   TRANSMEM    528    548       Helical. {ECO:0000256|RuleBase:RU365020}.
FT   TRANSMEM    560    580       Helical. {ECO:0000256|RuleBase:RU365020}.
FT   DOMAIN      165    335       Glyco_trans_2-like. {ECO:0000259|Pfam:
FT                                PF00535}.
FT   DOMAIN      585    681       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   743 AA;  83135 MW;  B5CB9C26C0419E4C CRC64;
     MSTAPEDILD AVDAEPPRRS RFDRLASHLI DGRILGSKPV TILLVLFALA SLFFVFTVPL
     AFGEQLTFAL CCFVCAMLFR RAKGHYATLV MIMLSVIATG RYMYWRLTET TYWERPLDAA
     WGLLLVSAEV YAALVLMLGY FQTAWPLKRK PLPLPADRSE WPTVDIFIPT YNEPLSVVKP
     TVYAAIALDY PKDKLSIHVL DDGRRPEFKA FCEEVGVAWT IRSHNRHAKA GNINEALKIT
     DGEYFAIFDC DHIPTRSFLQ VGLGWFLRDK KLSMLQTPHH FFSADPFEKN LGTFRKVPNE
     GELFYGLVQD GNDLWNATFF CGSCALLRRT MVEEIGGIAI ETVTEDAHTA LKLHRRGYTT
     AYLAIPQAAG LATESLGGHI GQRIRWARGM TQIFRIDNPL TGRGLTFGQR LCYLNAMMHF
     FYGIPRLVFL TAPLSFLFFN AHIIQAAAGT IAIFALPHMF HANVTNSRMQ QKFRHSFWSE
     VYESVLASYI TAPTLLALIN PKLGKFNVTA KGGRIEEQYF DWAISRPYLI LLALNLIGFI
     VGCVHIALNA SLHSEVQTTV LNLAWTGYNM LILGASVAAA REQRQVRATH RVAMRIPASL
     RFSTGRTLTC ETVDYAEGGL ALQLPAAIQV PLHEQVVVSL FRGQDEFVFP ADVTYAVPGR
     VGLKFGAMTR EQELDFVQST FARADAWTGW AEGREVDTPL KSFSHVMRVG VGGIGGLFEH
     LYADLRTLRS RRKAAANDTK NGK
//

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