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
//