ID U2FUR0_9BURK Unreviewed; 888 AA.
AC U2FUR0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=L810_3121 {ECO:0000313|EMBL:ERJ34335.1};
OS Burkholderia sp. AU4i.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1335308 {ECO:0000313|EMBL:ERJ34335.1, ECO:0000313|Proteomes:UP000016616};
RN [1] {ECO:0000313|EMBL:ERJ34335.1, ECO:0000313|Proteomes:UP000016616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU4i {ECO:0000313|EMBL:ERJ34335.1,
RC ECO:0000313|Proteomes:UP000016616};
RA Devi U., Khatri I., Kumar N., Kumar L., Singh D., Sharma D.,
RA Subramanian S., Saini A.K.;
RT "Genome Assembly of Burkholderia vietnamiensis AU4i.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:ERJ34335.1}.
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DR EMBL; ASSI01000197; ERJ34335.1; -; Genomic_DNA.
DR RefSeq; WP_021162968.1; NZ_ASSI01000197.1.
DR AlphaFoldDB; U2FUR0; -.
DR PATRIC; fig|1335308.3.peg.7380; -.
DR Proteomes; UP000016616; 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 52..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 498..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 579..888
FT /note="GH26"
FT /evidence="ECO:0000259|PROSITE:PS51764"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 720
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT ACT_SITE 824
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ SEQUENCE 888 AA; 98813 MW; 36E63211B6664D48 CRC64;
MKKLVASLAG GSVPDTADTA DTNETDTEAV RTDSQQADVP LVVPLMDSGT RIVFHILALC
WFVALGIFWR WWLRDEHYVD AFRFGVNCFV LFWTTFIPGY FIFIIRSAVV PNPALPVPRD
WRVAMVVTKA PSEPFDIVRT TLLAMLDQTY PHDTWLADED PSPETLDWCR EHGVFVSTRR
GIAAYHRASW PRRTRCKEGN LAYFYDMVGY DNYDFVSQLD ADHVPTRTYL EEMLRPFVDP
EVGYVSAPSI CDSNAAGSWS ARGRVNVEGP LHGTMQAGYA GGLAPLCIGS HYAVRCRALR
EIGGLGPELA EDHSTTMIFN SKGWRGMHAL NAIANGEGPR TFGDLATQEF QWSKSVMIIM
LRYTRHYFTG LPLKLKAQFL FCQLWYPLCA LAMAGGVVIP VVALLTGRVW AHVDYLTYLT
YALPLAVLLL CVVTWATRST QSCRPLNTKL LSWEGLSFVF ARWPWVVLGC ASAVFDFVRG
KEFPFKVTPK GGTIEQDAPL RVVAPYLLIS LFCSLPVVTV ENPRNAAGFY LFSTLTSILY
LVIAAVVAVN HGREQGLEWS AFRQMFFSRL PVRNALFVFA LAMLLAGIGL RAPKGWQAMM
WRSGLPAVVA PAPGEPVKQP ELGAYDPDNT LAANRDLAFD HVFVSWNAPD IRAEIDAAYR
NAQARNRSLM LTVEPWAAGD TRPGALLADI AHGRYDAQIA ATCSALAALK GPVFVRWGHE
MEADTGRYPW AIGDAPAYVD AYRRVVTTCR TMTDQLRYVW SPAGNRNLDD YFPGRGYVDA
VGLSVFDCPR CATWPAGGHA SAASILRTKY ERVTDYGLPV MITELGVDGS GSRKREALDE
LQRSLWRYPL LKAVVYFNAV DTPGAWPVHY VPDWRIAPTF LQTTVVAR
//
