ID A0A1M5CBH6_9BURK Unreviewed; 367 AA.
AC A0A1M5CBH6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase {ECO:0000313|EMBL:SHF52088.1};
GN ORFNames=SAMN02745117_02119 {ECO:0000313|EMBL:SHF52088.1};
OS Lampropedia hyalina DSM 16112.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Lampropedia.
OX NCBI_TaxID=1122156 {ECO:0000313|EMBL:SHF52088.1, ECO:0000313|Proteomes:UP000184327};
RN [1] {ECO:0000313|EMBL:SHF52088.1, ECO:0000313|Proteomes:UP000184327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16112 {ECO:0000313|EMBL:SHF52088.1,
RC ECO:0000313|Proteomes:UP000184327};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQUZ01000026; SHF52088.1; -; Genomic_DNA.
DR RefSeq; WP_073356654.1; NZ_FQUZ01000026.1.
DR AlphaFoldDB; A0A1M5CBH6; -.
DR STRING; 1122156.SAMN02745117_02119; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000184327; 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; cd06912; GT_MraY_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:UP000184327};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SHF52088.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 367 AA; 41230 MW; C64F129F54C7EA6F CRC64;
MLILCVFAFF ITTIISGLLV RRARRHARRY PGGMPQRFHK GDVPRIGGVA LACGMGCAAF
VGMFNTLRGD VANLNLGWWS IVWGLCMIPA VLGGLLEDLS QRMSVRWRFL LTFTSAALAV
WLLGASVPRL DIGWLDGTTW LWPWLGIGIA LLAVAGLPHA LNIIDGYNGL ACMVAIIVSL
ALAHVSLQVN DRALAAMFVV TAASSGGFLL WNYPRGLIFA GDSGAYLWGS ILSIGCILLV
QRHEEVSPWF PLLLLIYPVW ETLFSMYRKW VRGSSPGMAD ALHFHQLIYR RIVQRVFDDD
NEARDMLMRN NRTSPYLWAY TVLTVLPAVI FWHTSWVLML FCVFFAITYT AAYVAIVRFK
VPDWLRW
//
