ID C7NJS9_KYTSD Unreviewed; 266 AA.
AC C7NJS9;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase {ECO:0000313|EMBL:ACV06861.1};
GN OrderedLocusNames=Ksed_18590 {ECO:0000313|EMBL:ACV06861.1};
OS Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS (Micrococcus sedentarius).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC Kytococcus.
OX NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV06861.1, ECO:0000313|Proteomes:UP000006666};
RN [1] {ECO:0000313|EMBL:ACV06861.1, ECO:0000313|Proteomes:UP000006666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541
RC {ECO:0000313|Proteomes:UP000006666};
RX PubMed=21304632; DOI=10.4056/sigs.761;
RA Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL Stand. Genomic Sci. 1:12-20(2009).
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; CP001686; ACV06861.1; -; Genomic_DNA.
DR AlphaFoldDB; C7NJS9; -.
DR STRING; 478801.Ksed_18590; -.
DR KEGG; kse:Ksed_18590; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_3_2_11; -.
DR Proteomes; UP000006666; 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 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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACV06861.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..266
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002981007"
FT TRANSMEM 137..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 266 AA; 26600 MW; 868DD23417EEBEC8 CRC64;
MGGAVGVVVA RRLGVPVSAS WALATAALAA VGHLDDQHDL PASTRLGAQL ATGALLGAWE
GGTAGGALGA VGVPAVVNAV NFMDGINGIT GCTAVAWGLS AAGLGGVEAT QGCLTAGMAA
GFLPFNMPRA RMFLGDVGSY LFGASMAVTA LQAFLRAEDG ERVRRLLPAA APLTLYLADT
GTTLVRRARR GEPLFEAHRE HAYQRLVSDA GLAHWKVSTA VGLATGAAGL AARDPRVATV
ALPLLAGSYL ASPSVLAGNG LPVNAA
//
