ID A0A1H2PMN1_9BURK Unreviewed; 367 AA.
AC A0A1H2PMN1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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:SDV47815.1};
GN ORFNames=SAMN05216551_103318 {ECO:0000313|EMBL:SDV47815.1};
OS Chitinasiproducens palmae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Chitinasiproducens.
OX NCBI_TaxID=1770053 {ECO:0000313|EMBL:SDV47815.1, ECO:0000313|Proteomes:UP000243719};
RN [1] {ECO:0000313|Proteomes:UP000243719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS23 {ECO:0000313|Proteomes:UP000243719};
RA Varghese N., Submissions S.;
RL Submitted (SEP-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; FNLO01000003; SDV47815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2PMN1; -.
DR STRING; 1770053.SAMN05216551_103318; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000243719; 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:UP000243719};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDV47815.1};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 367 AA; 40540 MW; 8C2BB838362AC16A CRC64;
MQSLALGFLI SLLATLAIVR YAHLHKRFSA DSDLVGVQKF HSRPVPRVGG IGIVLGLLVS
AAQLWFSYPV VAQQILLLAA CGAPAFLSGL IEDLTKRVSP LLRLLATMAA ALLAYLALGI
HANRADLPFL DIALQYAAPS VLLTVVAVAG LANAVNIIDG FNGLASMVSM MMLVSLAYVA
FQVSDPVVLS SSLILMGAVF GFFVWNFPAG LIFLGDGGAY FLGFVLGELS ILLVMRNPQV
SAWYPVLMAM YPIFETCFSI YRKRFVRGMS PGIPDGVHLH MLVYKRLMRW AVGTREASAL
TQRNSYTSPY LWMLCLMAVL PATLFWRHTV VLVFFVAIFA ATYVWLYVSI VRFRTPRWMV
IRRHDRQ
//