ID S0NH21_9ENTE Unreviewed; 788 AA.
AC S0NH21;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=OMQ_00700 {ECO:0000313|EMBL:EOT30008.1};
OS Enterococcus saccharolyticus subsp. saccharolyticus ATCC 43076.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1139996 {ECO:0000313|EMBL:EOT30008.1, ECO:0000313|Proteomes:UP000014136};
RN [1] {ECO:0000313|EMBL:EOT30008.1, ECO:0000313|Proteomes:UP000014136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43076 {ECO:0000313|EMBL:EOT30008.1,
RC ECO:0000313|Proteomes:UP000014136};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus saccharolyticus ATCC_43076 (Illumina
RT only assembly).";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000122};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:EOT30008.1}.
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DR EMBL; AHYT01000002; EOT30008.1; -; Genomic_DNA.
DR RefSeq; WP_016174506.1; NZ_KE136523.1.
DR AlphaFoldDB; S0NH21; -.
DR STRING; 41997.RV16_GL001903; -.
DR PATRIC; fig|1139996.3.peg.695; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_011907_3_1_9; -.
DR OrthoDB; 9766299at2; -.
DR Proteomes; UP000014136; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR CDD; cd06421; CESA_CelA_like; 1.
DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR InterPro; IPR003919; Cell_synth_A.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009875; PilZ_domain.
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 Pfam; PF07238; PilZ; 1.
DR PRINTS; PR01439; CELLSNTHASEA.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF141371; PilZ domain-like; 1.
PE 4: Predicted;
KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000014136};
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 29..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..390
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT DOMAIN 533..620
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 788 AA; 91769 MW; F5D337201CBA55B0 CRC64;
MNLGEKEIVD VNPPIYQKES KIKVYRNQLW VLLTVILNII YLYWRIRYTL PLEFGIVSII
IGVSLIIVEV LGALESIVHY YNMHKIENPP VPDVPLELFP DVDIFIATYT EPMDLLYKTI
NGCKHLEYPD KSKVHIYLCD DGHRPEAREL AESMGIHYLD RPDNKGAKAG NLNHAMSKST
SPLILTMDAD MIPRRILLMR LVPYFVDAWL KNEGKDEKNQ IKMGFVQSPQ TFYNPDLFQY
FLFSENRIPN EQDYFYKDVQ VSRNRSNSVI YGGSNTLISR DALNDVGGFY EEAITEDFAT
GMLLQKKNYR CYAMNEELAS GLSPTDFPSL IQQRIRWARG CIQTGRKMHI FLSKGFSFSQ
KANYWASIWY WYAPIKRLIY IMSPIMFATF GYMVIKTDLL SILIFWLPMY LSSTITLRMM
SREIRTTKWT NIYETAMFPF LLFPVIEEFF GISLKKFKVT RKDGVNTEQS NNLLYALPFL
LFIILSIIGI VNIIYMILRN GSIGPIVVLF WLLVNLFNLV MATFFVLGRK FHRKSERVAI
SEPVVLKTEY EEIICETLDI SEGGISIWME NPIFIDEKNE ITLAITTDHY HAEVTGKLVH
VDEFKDGWKY AFQVEEYQES KADYMQMLYD RVHTLPKSLQ SSHSTFDDLR LNIVRRMQPT
IYFNRKSARI DMDEKIPLVT GGFVTIVNFN FEYFVTNSHD IEKEFECVLP NDVHFKCKYV
KNLINDNKLY QIVNIDEIAK NSQQMLLVTQ WAQQARKTKQ VEVEPQTDDT NLLVNDILGG
VDDENHTK
//
