ID A0A1G6F6D9_9FLAO Unreviewed; 366 AA.
AC A0A1G6F6D9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase {ECO:0000313|EMBL:SDB65122.1};
GN ORFNames=SAMN03097699_3051 {ECO:0000313|EMBL:SDB65122.1};
OS Flavobacteriaceae bacterium MAR_2010_188.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250295 {ECO:0000313|EMBL:SDB65122.1, ECO:0000313|Proteomes:UP000199442};
RN [1] {ECO:0000313|EMBL:SDB65122.1, ECO:0000313|Proteomes:UP000199442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2010_188 {ECO:0000313|EMBL:SDB65122.1,
RC ECO:0000313|Proteomes:UP000199442};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; LT629302; SDB65122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6F6D9; -.
DR STRING; 1250295.SAMN03097699_3051; -.
DR OrthoDB; 662756at2; -.
DR Proteomes; UP000199442; Chromosome i.
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:UP000199442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDB65122.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 366 AA; 41027 MW; 49144E336B59248A CRC64;
MNLLFNPQVL LDFFNEHRIL FSVFIFSTSF IITFLIIPKI IFVTFKRRLL TEVGSRSSHK
VSTPVFGGVA FFITIILILS VTQSMYQEYL IGNQIIAAVT ILFIVGLKDD LVVSTAKAKL
VSQIIAVTFV VFLPELNILS LKGFLGIYEI GFLNIFAMLF MLMVINGYNL IDGIDGLAAI
IGIIICGAFA YVYFTIHDNF YFLLSVTVIG SLAAFLRYNL SNTKKKLFMG DTGSLIIGFI
IGLLSLRFLT HRDIVTSTIG LLTENSVPII VAILCVLIFD TSRIVISRIL EKKHPFEADR
NHAHHILLDS GLSHLNSSLL LGAFNIVMII VFWSLGVYFS SFILAALLIL CFIAYFFVLN
KLKKRY
//
