MPRF_STAXY
ID MPRF_STAXY Reviewed; 841 AA.
AC Q93QY7;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 75.
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;
OS Staphylococcus xylosus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1288;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND HOST DEFENSE PEPTIDES RESISTANCE.
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=11342591; DOI=10.1084/jem.193.9.1067;
RA Peschel A., Jack R.W., Otto M., Collins L.V., Staubitz P., Nicholson G.,
RA Kalbacher H., Nieuwenhuizen W.F., Jung G., Tarkowski A., van Kessel K.P.M.,
RA van Strijp J.A.G.;
RT "Staphylococcus aureus resistance to human defensins and evasion of
RT neutrophil killing via the novel virulence factor MprF is based on
RT modification of membrane lipids with L-lysine.";
RL J. Exp. Med. 193:1067-1076(2001).
RN [2]
RP HOST DEFENSE PEPTIDES RESISTANCE.
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=12496209; DOI=10.1128/iai.71.1.546-549.2003;
RA Kristian S.A., Duerr M., van Strijp J.A.G., Neumeister B., Peschel A.;
RT "MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads
RT to protection against oxygen-independent neutrophil killing.";
RL Infect. Immun. 71:546-549(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.
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; AF145698; AAK58113.1; -; Genomic_DNA.
DR RefSeq; WP_047172427.1; NZ_LN554884.1.
DR AlphaFoldDB; Q93QY7; -.
DR SMR; Q93QY7; -.
DR STRING; 1288.SXYLSMQ121_1439; -.
DR KEGG; sxo:SXYL_01524; -.
DR eggNOG; COG0392; Bacteria.
DR eggNOG; COG2898; Bacteria.
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..841
FT /note="Phosphatidylglycerol lysyltransferase"
FT /id="PRO_0000096569"
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..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..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..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..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..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..489
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..841
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 841 AA; 96942 MW; 8C74A8AC44F00BB1 CRC64;
MTKELRSKLF TILKIAFALT LFTIVAITLY KELSHINLKD AIKSFSKINR FWLVALFLSG
GASIIVLSIY DVILAKTLKL KIGLAKTIRI GYIVNALNAV VGFGGFIGAS VRFLFYKNTT
DDKKALFHTI SIVLISMLTG LSLLSILVVI HVFDISHIFT PYPWVKWLMY VVALFLPIFV
VFTIIKPVQK THRLLGVYCT IVSGVEWFVA ALVLYMSMAI VGVQIPFATF MGIFILAALS
GLISFIPGGF GTFDLVVLLG LKALNVNEEA IVLGLSLYRF AYYLFPVLIA LILSTFEFRS
TAKRYWEDSR ILVPVKDMTS LLGSYQKDII ARIPSFAIAL LLLFTSLVFF LNNLTIIYDG
LYDPNHYIYY IIVSIHTCAC LLLLLNVIGV YKLSKRAILF SIISVLFIFI ATAYTYASFI
LLSWLTVIFI LLLVFYRRAR VIKRPFRYSK LLLSVITGAI ILYINHLVIK STFYSLEIYH
IEMLTSILRY YFWITILLVA IIVGVIVWWF EYRYRSSNSR DNIATCESII DKYNGNYLSH
LMYSGDKKFF INDNKDAFVM YRYHNNTYII LGDPIGNSES FYSLLEAFYK EAEYLGYDII
FYQVTDKYMS LYHSFGNQFF KLGEEAVINL TSFTTSGKKK RGLRATLNKL DDLGYSFEVL
EPPFSQQMIT DLKAISDDWL ADKNEMHFSV GSFDEHYISQ APIGVLKDNE QSVIAFCTLM
PTYYNGVISV DLIRWKQDIE LPLMDSLYLN MLLWSKDNNY EHFNMGMATL SNVGQIPYSF
YGERIAGRVF EHFNGLYRFQ GLRRYKEKFN PKWEPRFLVY RKHQSLWVSM LKVMRVIRKN
N
