MPRF_STAES
ID MPRF_STAES Reviewed; 840 AA.
AC Q8CPC0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=SE_1041;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04638.1; -; Genomic_DNA.
DR RefSeq; NP_764596.1; NC_004461.1.
DR RefSeq; WP_001831275.1; NZ_WBME01000040.1.
DR AlphaFoldDB; Q8CPC0; -.
DR SMR; Q8CPC0; -.
DR STRING; 176280.SE_1041; -.
DR EnsemblBacteria; AAO04638; AAO04638; SE_1041.
DR GeneID; 50018832; -.
DR KEGG; sep:SE_1041; -.
DR PATRIC; fig|176280.10.peg.1016; -.
DR eggNOG; COG0392; Bacteria.
DR eggNOG; COG2898; Bacteria.
DR HOGENOM; CLU_008255_7_1_9; -.
DR OMA; WEPRYMA; -.
DR Proteomes; UP000001411; 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.
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_0000096567"
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..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..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..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..415
FT /note="Extracellular"
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; 97219 MW; 8828931E94D5005E CRC64;
MTQELKSKLL SFFKFIFATA LFIFVIFTLY RELSHINFKE TFIQFGKINR LWLVLLFAGG
GLSLILLSLY DIILVKALKL KMPLIRVFRV SYIINALNSI IGFGGFIGAG VRAFVYKNYT
NDTKKLVQYI SIILVSMLTG LSLLSILVVL RIFNASHMID EISWVRWILY IVALFLPIFI
FYTVARPVDR NNRYMGVYCT VVSCVEWMAA ATVLYFAALI VDIHISFMTF VGIFVIAALS
GLVSFIPGGF GAFDLVVLLG LKSLGISEEK ILLALVLYRF AYYFVPVMIA LILSSFEFGN
TAKKYLDNSK YFIPVKDFTS FLRSYQKDIL AKVPSFSLAI LIFLTSIIFF INNLTIVYDG
LYDGNHFAYY IALAVQTSAC LLLILNVRGI YKGSRRAIIY AFISIILIAS ATIYTYASFL
LLSWLIIIFV LLILAYQRAQ VLKRPLRFKK LAVMLLLSIF ILYLNHILIS GTLYALDVYH
IEIDTSLLRY YFWMTIVIIM LLVGVIAWLF DYKYKCPHHS IDLTLCDAII QKYGGNYLSH
LVYSGDKDCF FNENKDSFIM YRYKSNALVV LGDPIGNTKS FESLLEAFYQ FAEYQGYEII
FYQISDQYMP LYHNFGNQFF KLGEEAIIDL TTFTTSGKKR RGFRATLNKF DDLNINFEII
EPPFTQDFFD ELKFVSDKWL DGRSEMHFSV GQFTQTYLSK APIGVMRDHS GKMIAFCSLM
PTYSNNAISV DLIRWLPELD LPLMDGLYLH MLLWSKEKGY KAFNMGMATL SNVGQLHYSY
LRERMAGRVF EHFNGLYRFQ GLRRYKEKYS PNWEPRFLVY QKHYSLWESM LKVMRVIRHK
