ID A0A1F7IHJ4_9BACT Unreviewed; 881 AA.
AC A0A1F7IHJ4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=A3A74_01410 {ECO:0000313|EMBL:OGK42846.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_35_13.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802055 {ECO:0000313|EMBL:OGK42846.1, ECO:0000313|Proteomes:UP000179270};
RN [1] {ECO:0000313|EMBL:OGK42846.1, ECO:0000313|Proteomes:UP000179270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGK42846.1}.
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DR EMBL; MGAF01000004; OGK42846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7IHJ4; -.
DR STRING; 1802055.A3A74_01410; -.
DR Proteomes; UP000179270; 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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 498..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 534..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 559..871
FT /note="GH26"
FT /evidence="ECO:0000259|PROSITE:PS51764"
FT ACT_SITE 702
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT ACT_SITE 814
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ SEQUENCE 881 AA; 102697 MW; 1018EFC02A3ABEAB CRC64;
MIKGTNNKLR VMNRLQSAIY LALVASAVFF TLRYFIWWIN LTHIPLNWTY ANLHFLDVLI
FITLTFAVFL PMLNDFGVWF ALWFMSKPKH IPIIKKYTVA FLTCYVPGKE PIDMLEKTLT
AMKKVRYEHD TWVLDEGDDS EVKLLCKRLD VKHFSRKCRL QYNQSEGKYR TKTKADNHNA
WLNQFEDNYD IIAQIDMDHI PEPDYFERTL GQFEDPKVGI ICMPQYYKNT DNWIARGSAE
QAYLFHGPIQ QGYYGCDMPF LIGTSHIYRR TAMKDIDGYA PTIVEDHLTG MLFYSRGWKG
VFVPEVLARG DGPTNWLDYF NQQMRWSFGL FEILFNHTPK ILDKLNWQQK INYFTAQLYY
FSGVSVFLGT VLTFFYLVFG INSAHMNLLI WLTYSVPTFI LGILIQIYVH QFTIDPKKEP
VYGIIGMFLN LGANLIYTLA FFKFIAGKKM QYMVTKKGSM AIDSKTPIEI FIPHLVMVFL
MTYALASSFV LKNNALQLRL WAVFSIISLS GVVGSSHLYY FYKRLEKLFN VKLFLRYSFV
AAAIVLVTFL ISGRNTIDGQ VERNYQKLPE IIHTVTPFPN VDLTGAMLGI SFSNSVYDEL
LHTEEITGLD YDLVGFYQAW GSENNQFDQS LAYAIKNKGS IPMITWEPWV PVASYDRTIE
QALQDKYHLR NIIRGDFDEY IKEYANSVRD YQNPVMIRFA HEMNGNWYPW GSTFNTPSEY
IMAWRHVHDI FTEVGTPNVA WIWAPNEEYV EPLVPFSHSS EVFYPGDKYV DWVGVSSFNW
AGRYKQNIWR KPEDLFESTI SKLKQYQKPI IITETASSET IGYPGQKALW IEQMAEYVKL
NPEIKGLVWF NVNDNNIDWS IESSDSSLKS FINWFGDSYF N
//
