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Database: UniProt
Entry: A0A1T4T9P6_9BACT
LinkDB: A0A1T4T9P6_9BACT
Original site: A0A1T4T9P6_9BACT 
ID   A0A1T4T9P6_9BACT        Unreviewed;      1239 AA.
AC   A0A1T4T9P6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE            EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN   ORFNames=SAMN04488128_104207 {ECO:0000313|EMBL:SKA36999.1};
OS   Chitinophaga eiseniae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=634771 {ECO:0000313|EMBL:SKA36999.1, ECO:0000313|Proteomes:UP000190367};
RN   [1] {ECO:0000313|EMBL:SKA36999.1, ECO:0000313|Proteomes:UP000190367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22224 {ECO:0000313|EMBL:SKA36999.1,
RC   ECO:0000313|Proteomes:UP000190367};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; FUWZ01000004; SKA36999.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4T9P6; -.
DR   STRING; 634771.SAMN04488128_104207; -.
DR   OrthoDB; 9802773at2; -.
DR   Proteomes; UP000190367; 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; 2.
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; 2.
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, ECO:0000313|EMBL:SKA36999.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        365..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        441..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        469..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        502..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        533..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          530..828
FT                   /note="GH26"
FT                   /evidence="ECO:0000259|PROSITE:PS51764"
FT   ACT_SITE        671
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        776
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ   SEQUENCE   1239 AA;  139911 MW;  0AA697CFD9388AE3 CRC64;
     MREKEQPAPV TPPSRRELFT LRLMILLGTV SIGVLLTVLF RRTQIGYAPL YWVLMAAITF
     NCLTILHEWY HYAAIRIPPS PPPQHPFTVD VLTTYFPGEP YDMIVNTLTA IRAMTYPHTA
     WLCDEANDPY LREVCARLGV RHVTRTNRKD AKAGNINNAL QYATGELCVV MDPDHVPAPD
     FLDAVVHHFN DPGIGFVQIV QAYSNLGDNL IAKGAAQQTF QFYGPIMSTM NSYGTVLAIG
     ANCTFRRAAL DSIGGHASGL AEDMHTAMHL HAKGWKSIYV PAVLTRGLVP NTLSAYYAQQ
     LKWARGTFEL LVTTYPRLFR QFTWLQRLHY GTIPLHYLSG VVFLINFLVP VLSLVTGYIP
     FRADLVQFSL LAFPAIASII LIRHYVQRWV MEETERGFHV VGGLLFIGTW WIYLLGLIYT
     IARKRVPYLP TPKDDSGPDD WRLNLPNIVI LVISLAAIIY GLSHDWNPYS LFMAGIAGIN
     CLIMVFNIMA SLQLKKIPAR YGWVKTILTL PLFLKRQFWI FRHLHLYTGI RKLGLPLLLV
     VIVLSWYFTA GRRQAPVSVL PSRQDVFYTG AYNPSGEGLP RTQITSLYIA WGDGQDHLLP
     DSLTAIYNSG SIPMVTWEPW TSRFTHNAGQ VQQERKVMSL IPTGIFDSYL EQFADQVKAL
     NRPLFLRFAH EPDNPAYPWS PTGGNTPEEY GRAWRYVHTL FLRRGAINAV WVWSPWKASN
     AEKYFPGKEF VDWIGVTALN YGPAHGGGAW YSFEALYQPF HQLPLFRSGL PVMIAEMGSA
     SDAGDQARWF SDAFLAISNR FPEVHAQVFF NTGHDVNVVK GDTARYLDWS IRQPGQLLAV
     LDSFPRLRGP AALNVTAIAG AATVAPVPHH PLPDNLRGLR YQKGEDWFRN RYALTRRETA
     HDLQQMQQLG VNTIRRYGPG VYDRNVLSEA RSHGIHIHYG FWLPDVTDMD KDSVMLARAQ
     RDILRNIARR RNDTVITAWQ IGNNAWQQLG QYHFKPALLY QQQRYLRWLE GLARAIKATD
     PSRPVTTDVL FQSATAPLLP WLRQQLPAID AFGIETIGDT TGLAALLSGN VPCFISKIPV
     ASYAALSPVP AFITTWQDLE TRDYVTFDGL IDHRGRHKPA WEQLSGLWSQ RSALPSLPKV
     KILRPSRTTL PGSRLTYHAL VSTGAGWRFA DPGKDQLQFE WYLVQTDRYG NPFHLQPVGK
     GASFTLTVPD KPMQYRLYLE AARDSSVVTG ITTLNTPLY
//
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