ID   MPRF_STAAW              Reviewed;         840 AA.
AC   Q8NWU7;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Phosphatidylglycerol lysyltransferase;
DE            EC=2.3.2.3;
DE   AltName: Full=Lysylphosphatidylglycerol synthase;
DE            Short=LPG synthase;
DE   AltName: Full=Multiple peptide resistance factor;
GN   Name=mprF; OrderedLocusNames=MW1247;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Catalyzes the transfer of a lysyl group from L-lysyl-
CC       tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces
CC       lysylphosphatidylglycerol (LPG), a major component of the bacterial
CC       membrane with a positive net charge. LPG synthesis contributes to
CC       bacterial virulence as it is involved in the resistance mechanism
CC       against cationic antimicrobial peptides (CAMP) produces by the host's
CC       immune system (defensins, cathelicidins) and by the competing
CC       microorganisms (bacteriocins). In fact, the modification of anionic
CC       phosphatidylglycerol with positively charged L-lysine results in
CC       repulsion of the peptides (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-
CC         tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-
CC         glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696,
CC         Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the LPG synthase family. {ECO:0000305}.
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; BA000033; BAB95112.1; -; Genomic_DNA.
DR   RefSeq; WP_001071152.1; NC_003923.1.
DR   AlphaFoldDB; Q8NWU7; -.
DR   SMR; Q8NWU7; -.
DR   EnsemblBacteria; BAB95112; BAB95112; BAB95112.
DR   KEGG; sam:MW1247; -.
DR   HOGENOM; CLU_008255_7_1_9; -.
DR   OMA; WEPRYMA; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050071; F:lysyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR022791; L-PG_synthase/AglD.
DR   InterPro; IPR024320; LPG_synthase_C.
DR   Pfam; PF09924; LPG_synthase_C; 1.
DR   Pfam; PF03706; LPG_synthase_TM; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR00374; TIGR00374; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Lipid metabolism; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..840
FT                   /note="Phosphatidylglycerol lysyltransferase"
FT                   /id="PRO_0000096565"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..52
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..89
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..128
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..271
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..369
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        391..394
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        437..450
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        472..489
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        511..840
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   840 AA;  96893 MW;  E21C61E1B6778823 CRC64;
     MNQEVKNKIF SILKITFATA LFIFVVITLY RELSGINFKD TLVEFSKINR MSLVLLFIGG
     GASLVILSMY DVILSRALKM DISLGKVLRV SYIINALNAI VGFGGFIGAG VRAMVYKNYT
     HDKKKLVHFI SLILISMLTG LSLLSLLIVF HVFDASLILD KITWVRWVLY VVSFFLPLFI
     IYSMVRPPDK NNRFVGLYCT LVSCVEWLAA AVVLYFCGVI VDAHVSFMSF IAIFIIAALS
     GLVSFIPGGF GAFDLVVLLG FKTLGVPEEK VLLMLLLYRF AYYFVPVIIA LILSSFEFGT
     SAKKYIEGSK YFIPAKDVTS FLMSYQKDII AKIPSLSLAI LVFFTSMIFF VNNLTIVYDA
     LYDGNHLTYY ILLAIHTSAC LLLLLNVVGI YKQSRRAIIF AMISILLITV ATFFTYASYI
     LITWLAIIFV LLIVAFRRAR RLKRPVRMRN IVAMLLFSLF ILYVNHIFIA GTLYALDIYT
     IEMHTSVLRY YFWLTILIIA IIIGMIAWLF DYQFSKVRIS SKIEDCEEII NQYGGNYLSH
     LIYSGDKQFF TNENKTAFLM YRYKASSLVV LGDPLGDENA FDELLEAFYN YAEYLGYDVI
     FYQVTDQHMP LYHNFGNQFF KLGEEAIIDL TQFSTSGKKR RGFRATLNKF DELNISFEII
     EPPFSTEFIN ELQHVSDLWL DNRQEMHFSV GQFNEEYLSK APIGVMRNEE NEVIAFCSLM
     PTYFNDAISV DLIRWLPELD LPLMDGLYLH MLLWSKEQGY TKFNMGMATL SNVGQLHYSY
     LRERLAGRVF EHFNGLYRFQ GLRRYKSKYN PNWEPRFLVY RKDNSLWESL SKVMRVIRHK