ID G7VA90_THELD Unreviewed; 307 AA.
AC G7VA90;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Glycosyl transferase, family 4, conserved region {ECO:0000313|EMBL:AER66790.1};
GN OrderedLocusNames=Tlie_1057 {ECO:0000313|EMBL:AER66790.1};
OS Thermovirga lienii (strain ATCC BAA-1197 / DSM 17291 / Cas60314).
OC Bacteria; Synergistota; Synergistia; Synergistales; Thermovirgaceae;
OC Thermovirga.
OX NCBI_TaxID=580340 {ECO:0000313|EMBL:AER66790.1, ECO:0000313|Proteomes:UP000005868};
RN [1] {ECO:0000313|Proteomes:UP000005868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314
RC {ECO:0000313|Proteomes:UP000005868};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Saunders E.,
RA Kyrpides N., Mavromatis K., Ivanova N., Last F.I., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Thermovirga lienii DSM 17291.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AER66790.1, ECO:0000313|Proteomes:UP000005868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314
RC {ECO:0000313|Proteomes:UP000005868};
RX PubMed=22768366; DOI=10.4056/sigs.2726028;
RA Goker M., Saunders E., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Genome sequence of the moderately thermophilic, amino-acid-degrading and
RT sulfur-reducing bacterium Thermovirga lienii type strain (Cas60314(T)).";
RL Stand. Genomic Sci. 6:230-239(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR600715-1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; CP003096; AER66790.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VA90; -.
DR STRING; 580340.Tlie_1057; -.
DR KEGG; tli:Tlie_1057; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_2_3_0; -.
DR OrthoDB; 9805475at2; -.
DR Proteomes; UP000005868; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR CDD; cd06853; GT_WecA_like; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR PANTHER; PTHR22926:SF3; UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYL 1-PHOSPHATE TRANSFERASE; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|PIRSR:PIRSR600715-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005868};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AER66790.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 307 AA; 33519 MW; 350B014884650917 CRC64;
MATQAIVLSW KNAAFLSLLF FAWGIAATPL SIALAKTFRI VDMPGGRKKH KGIIPRGGGL
TCWIGYLFLS FVLLGIYPEM APIATGATVV FLVGYVDDMR QLPAWVKLFF HLLASTFIVC
FLPVSLPLRA LLVLWIAGAT NAYNLIDGVN GLALSLFMLS CVLGAITTKI GIFFPLAAMA
LGVFFWNFPV AKTFLGDGGS TLLGFLCMGH LSFAMCPLLV ERSPIIIVLS LFLIGGVPFL
DTFWVASRRI VLRKSPFTPD RGHIHFILLD KGLKIEQTLF LLLLIHGCII AMGYGLILGK
ISLLSYF
//
