ID T2N890_PORGN Unreviewed; 221 AA.
AC T2N890;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glycosyltransferase, group 4 family {ECO:0000313|EMBL:EOA10155.1};
GN ORFNames=A343_2161 {ECO:0000313|EMBL:EOA10155.1};
OS Porphyromonas gingivalis JCVI SC001.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1195243 {ECO:0000313|EMBL:EOA10155.1};
RN [1] {ECO:0000313|EMBL:EOA10155.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCVI SC001 {ECO:0000313|EMBL:EOA10155.1};
RX PubMed=23564253; DOI=10.1101/gr.150433.112;
RA McLean J.S., Lombardo M.J., Ziegler M.G., Novotny M., Yee-Greenbaum J.,
RA Badger J.H., Tesler G., Nurk S., Lesin V., Brami D., Hall A.P., Edlund A.,
RA Allen L.Z., Durkin S., Reed S., Torriani F., Nealson K.H., Pevzner P.A.,
RA Friedman R., Venter J.C., Lasken R.S.;
RT "Genome of the pathogen Porphyromonas gingivalis recovered from a biofilm
RT in a hospital sink using a high-throughput single-cell genomics platform.";
RL Genome Res. 23:867-877(2013).
RN [2] {ECO:0000313|EMBL:EOA10155.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCVI SC001 {ECO:0000313|EMBL:EOA10155.1};
RA McLean J., Yee-Greenbaum J., Durkin A.S., Lasken R.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:EOA10155.1}.
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DR EMBL; APMB01000213; EOA10155.1; -; Genomic_DNA.
DR AlphaFoldDB; T2N890; -.
DR PATRIC; fig|1195243.10.peg.391; -.
DR HOGENOM; CLU_1249691_0_0_10; -.
DR Proteomes; UP000016542; 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 InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
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.
DR PROSITE; PS01348; MRAY_2; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EOA10155.1};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 221 AA; 24828 MW; 8D14B52A3E1B7668 CRC64;
MCKFQGWAEE MILFLLLLFA TSILSYIALR RLSRMVYAQS VFDQENERTV HKGAIPRLGG
VIFFPVITLT VSLFLAINSV LSISIHFPLE EFYDLLFLLP AMILLYAIGV IDDLVGLSYR
QKFKAQILSS SILFLSGVSL SGLDGLLFIE ELPKILQYPI VVFFFLMVIN SINLIDGIDG
LATSLVLLGM LFYIPFFIYV NMYLYVIICV SVIGCLGAFF G
//
