ID A0A239CTT5_9BACT Unreviewed; 365 AA.
AC A0A239CTT5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase {ECO:0000313|EMBL:SNS23520.1};
GN ORFNames=SAMN06296052_103243 {ECO:0000313|EMBL:SNS23520.1};
OS Pontibacter ummariensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1610492 {ECO:0000313|EMBL:SNS23520.1, ECO:0000313|Proteomes:UP000198432};
RN [1] {ECO:0000313|Proteomes:UP000198432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NKM1 {ECO:0000313|Proteomes:UP000198432};
RA Varghese N., Submissions S.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZOQ01000003; SNS23520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239CTT5; -.
DR Proteomes; UP000198432; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000198432};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SNS23520.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 365 AA; 39527 MW; 5556BFFA7B2BBA25 CRC64;
MLVLTGAAFL YFTLELMEQR ILPLVLASSW AFLIAVFAVP SIIRVAHLKN ILDKPNLRTM
HGESTPRLGG MAMFAGFMSA LTIFTGLNNG VQQLLAGCII LFFIGLKDDM ITISALKKFA
VQVLATGIVM FMGDIRITSF QGIFGLWELE LGASYAFTFF VIVGITNAIN LIDGLDGLAG
TIVLIASFTF GLCFFFYGGT AYSSYASVAF CLIGGVLGFL RYNFHKATIF MGDTGSLLCG
FILSVLAIQF IEMRAVPATP SVALGVLFVP LFDTVRVMLI RAMSGKSPFA PDKNHVHHRL
TAMGLGQVTT VLVLGSVNTL AILFVLGFGE WGNHYILLVL LVFSAILSAL LEFNRLRSAQ
VVSKV
//
