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Database: UniProt
Entry: F0GCV2_9BURK
LinkDB: F0GCV2_9BURK
Original site: F0GCV2_9BURK 
ID   F0GCV2_9BURK            Unreviewed;       880 AA.
AC   F0GCV2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE            EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN   ORFNames=B1M_30370 {ECO:0000313|EMBL:EGD00685.1};
OS   Burkholderia sp. TJI49.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=987057 {ECO:0000313|EMBL:EGD00685.1, ECO:0000313|Proteomes:UP000003049};
RN   [1] {ECO:0000313|EMBL:EGD00685.1, ECO:0000313|Proteomes:UP000003049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TJI49 {ECO:0000313|EMBL:EGD00685.1,
RC   ECO:0000313|Proteomes:UP000003049};
RX   PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA   Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT   "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT   isolated from dieback affected mango orchards.";
RL   World J. Microbiol. Biotechnol. 29:2033-2044(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01100}.
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:EGD00685.1}.
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DR   EMBL; AEXE01001850; EGD00685.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0GCV2; -.
DR   PATRIC; fig|987057.7.peg.4755; -.
DR   BioCyc; BSP987057:G10O5-880-MONOMER; -.
DR   Proteomes; UP000003049; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06421; CESA_CelA_like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR022790; GH26_dom.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
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; PF02156; Glyco_hydro_26; 1.
DR   Pfam; PF13632; Glyco_trans_2_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   3: Inferred from homology;
KW   Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01100};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01100};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        45..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        376..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        410..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        448..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        490..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        518..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        562..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          585..880
FT                   /note="GH26"
FT                   /evidence="ECO:0000259|PROSITE:PS51764"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        712
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        816
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ   SEQUENCE   880 AA;  97575 MW;  1FF81B53556F2086 CRC64;
     MKKLVASLAG GPEAETGDAG AAPADTLRRE APLLVPLMDS GTKVIFQILA LCWFVALGIF
     WRWWLRDEHY VDAFRFGVNG FVLFWTTFIP GYFIFIIRSA VVPNPEVAVP RDWRVAMVVT
     KAPSEPFAIV RTTLLAMLDQ TYPHDTWLAD EDPTPETLEW CRQHGVRVST RRGVADYHRT
     SWPRRTRCKE GNLAYFYDMY GYDNYDFVSQ LDADHVPTRT YLEEMLRPFV DPAVGYVSAP
     SICDSNAAES WSARGRVNVE GPLHGTMQAG YAGGLAPLCI GSHYAVRCRA LREIGGLGPE
     LAEDHSTTMI FNAKGWRGMH ALNAIANGEG PRTFADLATQ EFQWSKSVMI IMLRYTRHYF
     GGLPLKLKAQ FLFCQLWYPL CALAMAGSVV IPVVALLTGR VWAHVDYLSY LTYALPLAVL
     ILCVVTWATH ATQSCRPLNT KLLSWEGLSF VFARWPWVVL GCASAIVDCL RGKEFAFKVT
     PKGGAIEQDA PLRVVAPYLL ISMFCSVPVV AVENAHNAAG FYLFSTLTSI LYLVIAAVVA
     VNHGKEQGLA ASTLAQMFFS RLPVRNALFV FALAMLLAGI GLRAPQGWRA VTWRSDVPEL
     LAPAPGQRVK QPALGAYDPD STFSADANLA FDHVFVSWNA PDLDTQIDRA YRDAQARHRS
     LMVTVEPWAL DGSRKGALLD DIAQGRYDAR IAATCSALAA LQAPVFVRWG HEMETDTGRY
     PWAIGDASGY VDAYRRVVTA CRAMTDKLRF VWSPAGNRNL DDYFPGRGYA DVIGLSVFDC
     PRCAVWPAGG RSSAASVLRV KYARVADYGL PVMVTELGVD GSDARKRDEL DEFQRSLWRY
     PLLKAVLYFN AVDTPGAWPA HYVPDWRIEP AFLPAEVVAK
//
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