ID   MPRF_STAAR              Reviewed;         840 AA.
AC   Q6GH45;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, 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=SAR1372;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
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DR   EMBL; BX571856; CAG40370.1; -; Genomic_DNA.
DR   RefSeq; WP_001071160.1; NC_002952.2.
DR   AlphaFoldDB; Q6GH45; -.
DR   SMR; Q6GH45; -.
DR   KEGG; sar:SAR1372; -.
DR   HOGENOM; CLU_008255_7_1_9; -.
DR   OMA; WEPRYMA; -.
DR   OrthoDB; 542304at2; -.
DR   Proteomes; UP000000596; 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_0000096562"
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;  96786 MW;  E52479843A21AEF6 CRC64;
     MNQEVKNKIF SILKITFATA LFIFVVITLY RELSGINFKD TLVEFSKINR MSLVLLFIGG
     GASLVILSMY DVILSRALKM DISLGKVLRV SYIINALNAI VGFGGFIGAG VRAMVYKNYT
     HDKKKLVHFI SLILISMLTG LSLLSLLIVF HVFDASLILN KITWVRWVLY AVSLFLPLFI
     IYSMVRPPDK NNRYVGLYCT LVSCVEWLAA AVVLYFCGVI VDVHVSFMSF IAIFIIAALS
     GLVSFIPGGF GAFDLVVLLG FKTLGVPEEK VLLMLLLYRF AYYFVPVIIA LILSSFEFGT
     SAKKYIEGSK YFIPAKDVTS FLMSYQKDII AKIPSLSLAI LVFFTSMIFF VNNLTIVYDA
     LYDGNHLTYY LLLAIHTSAC LLLLLNVVGI YKQSRRAIIY AMISIILIIV ATLFTYASYI
     LITWLVIIFA LLIVAFRRAR RLKRPIRMRN LVAMLLFSIF ILYINHIFIA GTFYALDVYT
     IEMHTSVLKY YFWITILIIA IIVGAIAWLF DYQFSKVRIS SNIEECEEII DQYGGNYLSH
     LIYSGDKQFF TNEDKNAFLM YRYKASSLVV LGDPIGDENA FDELLEAFYN YAEYLGYDVI
     FYQVTDQHMP LYHNFGNQFF KLGEEAIIDL TQFSTSGKKR RGFRATLNKF DELNISFEII
     EPPFSTEFIN ELQHVSDLWL DNRQEMHFSV GQFNETYLSK APIGVMRNEN NEVIAFCSLM
     PTYFNDAISV DLIRWLPELD LPLMDGLYLH MLLWSKEQGY TKFNMGMATL SNVGQLHYSY
     LRERLAGRVF EHFNGLYRFQ GLRRYKSKYN PNWEPRFLVY RKDNSLWESL SKVMRVIRHK