MPRF_STAHJ
ID MPRF_STAHJ Reviewed; 840 AA.
AC Q4L667;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 116.
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; Synonyms=fmtC; OrderedLocusNames=SH1549;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04858.1; -; Genomic_DNA.
DR RefSeq; WP_011275840.1; NC_007168.1.
DR AlphaFoldDB; Q4L667; -.
DR SMR; Q4L667; -.
DR STRING; 279808.SH1549; -.
DR PRIDE; Q4L667; -.
DR EnsemblBacteria; BAE04858; BAE04858; SH1549.
DR GeneID; 58062254; -.
DR KEGG; sha:SH1549; -.
DR eggNOG; COG0392; Bacteria.
DR eggNOG; COG2898; Bacteria.
DR HOGENOM; CLU_008255_7_1_9; -.
DR OMA; WEPRYMA; -.
DR OrthoDB; 542304at2; -.
DR Proteomes; UP000000543; 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_0000096568"
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..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..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..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..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..490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..840
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 840 AA; 96891 MW; BF668DC08E3237CC CRC64;
MTEELKNRLL SILKFVFAAV LFIAVVATLY HELAHINFKQ TLEAFSKINR WYLVGLFICG
GSAMILLSLY DLILVKGLKL DIPLIRVFKI SYIINALNAI VGFGGFIGAG FRAFIYKNYT
TDRKKLVHAI SIILISMLMG LSLLSILVVL HIFDASHIIN KVSWVRWILY VVALFLPLFI
AYTMINPIDR NNKYLGVYCT LVSSFEWLAA ATVLYLSTVI VDINIAFTTV IGIFIIAALS
GLVSFIPGGF GAFDLVVLLG LKSLGVPEEK VLLALLLYRF AYYFVPVIIA LILSTFEFGS
SARKYFEESK YFVPARDVTS FLFSYQKDII AKIPSFALAT LVLITSFVFF INNITIVYDG
LYDDHHFAYY IMLSVHTSAC LLLLINVRGV FKQSRRAILF VMISLVLIFS ATIYTYASLI
LLSWILLIFI LLILAYRRSK VMKRPFRLKR LIFTIILSML VLYVNHFIIS ETLYALDIYH
IEMDTSLLKY YFWLTILVVV ILVGIVAWLL GSRYTRPHQL EDLSRCKSII ETYGGNYLSH
LIYSGDKDVF MHEAQQAFLM YRYKGNALVV LGDPIGDTKA FQSLLIDFYN YGEKLGYDII
FYQVSDRFMP LYHNFGNQFF KLGEEAIIDL TQFTTSGKKR RGFRATLNKF DDLNIQFEIL
EPPFSKDLIF QLKQVSNQWL DGRNEMHFSV GQFTEEYLQQ APIGIMKNEE GKVIAFCTLM
PTYYNEAISV DLIRWLPDLD LPLMDGLYLH MLLWGKDKGY KAFNMGMATL SNVGQLNYSY
PRERVAGRVF EHFNGLYRFQ GLRKYKEKYS PNWEPRFLVY RKDSSLWYSM LKVMRVIRHK
