ID A0A1F5H3M6_9BACT Unreviewed; 417 AA.
AC A0A1F5H3M6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
DE Flags: Fragment;
GN ORFNames=A3A49_01445 {ECO:0000313|EMBL:OGD98655.1};
OS Candidatus Curtissbacteria bacterium RIFCSPLOWO2_01_FULL_38_11b.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1797725 {ECO:0000313|EMBL:OGD98655.1, ECO:0000313|Proteomes:UP000176740};
RN [1] {ECO:0000313|EMBL:OGD98655.1, ECO:0000313|Proteomes:UP000176740}
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 -!- 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:OGD98655.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFBO01000006; OGD98655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5H3M6; -.
DR STRING; 1797725.A3A49_01445; -.
DR Proteomes; UP000176740; 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:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR001173; Glyco_trans_2-like.
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; PF13632; Glyco_trans_2_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916};
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 285..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..329
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGD98655.1"
FT NON_TER 417
FT /evidence="ECO:0000313|EMBL:OGD98655.1"
SQ SEQUENCE 417 AA; 47219 MW; B80484E9EC611277 CRC64;
NVIERMLKAV TSFKWHVIAS KQGIDIANYE VIVIDDSTDQ TTQKGLNFLN AAGYSLSRSY
QDEKLEIITG VSQKDSKWPN VKYIHRFSRS GFKGAALAKA LEETDRRAEY VVIFDADFVP
YPDTLEQFVK HFAAIEQNEN INSQKIAAIQ GYQWHVLNKS ENWITKGVRS EYAGSYVVER
SAIELYGGLK MIAGSVYAIK RNILDKFGWG TSITEDLELT LKLYAAGYKV AYTPYIQAPA
EAVSTLKRLI RQRMRWAEGH SFNIHNQFKA ITASPHLTFK EKLEFAFLVP YYLQAAFFIA
GTFAWFVSEV IFKVNLPYWS AALGWSLVFS NFLALPLTNL LGLFLEQSEE KDYVGVASFV
LLSYLVAPFQ AYAAVKGFLE KEEGPWFRTP KTGIVTDTFG RLVIDKWSLS LPFGKPA
//