MPRF_STAAM
ID MPRF_STAAM Reviewed; 840 AA.
AC Q99UB9;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=SAV1360;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB57522.1; -; Genomic_DNA.
DR RefSeq; WP_001071136.1; NC_002758.2.
DR AlphaFoldDB; Q99UB9; -.
DR SMR; Q99UB9; -.
DR PaxDb; Q99UB9; -.
DR EnsemblBacteria; BAB57522; BAB57522; SAV1360.
DR KEGG; sav:SAV1360; -.
DR HOGENOM; CLU_008255_7_1_9; -.
DR OMA; WEPRYMA; -.
DR PhylomeDB; Q99UB9; -.
DR BioCyc; SAUR158878:SAV_RS07330-MON; -.
DR Proteomes; UP000002481; 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_0000096560"
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; 96865 MW; D51F0DC244D92877 CRC64;
MNQEVKNKIF SILKITFATA LFIFVAITLY 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
