MPRF_BACSU
ID MPRF_BACSU Reviewed; 856 AA.
AC C0H3X7; O31565; O52961; Q79EW4;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Phosphatidylglycerol lysyltransferase;
DE EC=2.3.2.3;
DE AltName: Full=Lysylphosphatidylglycerol synthase;
DE Short=LPG synthase;
GN Name=mprF; Synonyms=yfiW, yfiX; OrderedLocusNames=BSU08425;
GN ORFNames=BSU08420, BSU08430;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8946165; DOI=10.1093/dnares/3.4.257;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 27.8-kb nucleotide sequence of the 79 degrees-
RT 81 degrees region of the Bacillus subtilis genome containing the sspE
RT locus.";
RL DNA Res. 3:257-262(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=12427923; DOI=10.1099/00221287-148-11-3331;
RA Staubitz P., Peschel A.;
RT "MprF-mediated lysinylation of phospholipids in Bacillus subtilis
RT - protection against bacteriocins in terrestrial habitats?";
RL Microbiology 148:3331-3332(2002).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15743965; DOI=10.1128/jb.187.6.2163-2174.2005;
RA Nishibori A., Kusaka J., Hara H., Umeda M., Matsumoto K.;
RT "Phosphatidylethanolamine domains and localization of phospholipid
RT synthases in Bacillus subtilis membranes.";
RL J. Bacteriol. 187:2163-2174(2005).
RN [5]
RP FUNCTION IN LPG SYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / CU1065;
RX PubMed=18820022; DOI=10.1128/jb.00720-08;
RA Salzberg L.I., Helmann J.D.;
RT "Phenotypic and transcriptomic characterization of Bacillus subtilis
RT mutants with grossly altered membrane composition.";
RL J. Bacteriol. 190:7797-7807(2008).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / CU1065;
RX PubMed=19164152; DOI=10.1128/aac.01329-08;
RA Hachmann A.-B., Angert E.R., Helmann J.D.;
RT "Genetic analysis of factors affecting susceptibility of Bacillus subtilis
RT to daptomycin.";
RL Antimicrob. Agents Chemother. 53:1598-1609(2009).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
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), one of the components of the bacterial
CC membrane with a positive net charge. LPG synthesis contributes to the
CC resistance to cationic antimicrobial peptides (CAMPs) and likely
CC protects B.subtilis against its own CAMPs and against those produced by
CC competiting microorganisms (bacteriocins). In fact, the modification of
CC anionic phosphatidylglycerol with positively charged L-lysine results
CC in repulsion of the peptides. {ECO:0000269|PubMed:18820022}.
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 {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Localized in the septal membrane.
CC {ECO:0000269|PubMed:15743965}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lack lysyl-
CC phosphatidylglycerol in their membranes. They also display an increased
CC sensitivity to the antibiotics nisin and daptomycin (PubMed:18820022,
CC PubMed:19164152). Cells appear normal, no effect on flotillin cluster
CC numbers or size (PubMed:27362352). {ECO:0000269|PubMed:18820022,
CC ECO:0000269|PubMed:19164152, ECO:0000269|PubMed:27362352}.
CC -!- SIMILARITY: Belongs to the LPG synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24463.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
CC Sequence=BAA24464.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA24464.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; D85082; BAA24463.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D85082; BAA24464.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAX52582.1; -; Genomic_DNA.
DR PIR; A69805; A69805.
DR RefSeq; WP_003242495.1; NZ_JNCM01000032.1.
DR RefSeq; YP_003097695.1; NC_000964.3.
DR AlphaFoldDB; C0H3X7; -.
DR SMR; C0H3X7; -.
DR STRING; 224308.BSU08425; -.
DR EnsemblBacteria; CAX52582; CAX52582; BSU_08425.
DR GeneID; 8303094; -.
DR KEGG; bsu:BSU08425; -.
DR PATRIC; fig|224308.179.peg.910; -.
DR eggNOG; COG0392; Bacteria.
DR eggNOG; COG2898; Bacteria.
DR InParanoid; C0H3X7; -.
DR OMA; WEPRYMA; -.
DR PhylomeDB; C0H3X7; -.
DR BioCyc; BSUB:BSU08425-MON; -.
DR BRENDA; 2.3.2.3; 658.
DR Proteomes; UP000001570; 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:0016755; F:aminoacyltransferase activity; IBA:GO_Central.
DR GO; GO:0050071; F:lysyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055091; P:phospholipid homeostasis; IBA:GO_Central.
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 1: Evidence at protein level;
KW Antibiotic resistance; Cell membrane; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..856
FT /note="Phosphatidylglycerol lysyltransferase"
FT /id="PRO_0000390919"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 856 AA; 96322 MW; 4C4ED139433B0F40 CRC64;
MLIKKNALSI LKIVFPIAVL LFVIYQSKKE LTNLSFKRTL MVINGLERTD LFMLVLIGLL
AVAAMSLYDY VLKYSLRLSI TNGKVFRVSW IANSFNNVLG FGGLAGVGLR MMFYKEHTKD
HKALVKGIAW LTSSMLLGLS VFSIFVAARV LPVDEVIHEK PWLWAVVIGF ALILPLSLAV
SKIKDRKAGD EENADKVKNP IFAYIGASVV EWLMAGTVIY FALFAMGIHA DIRYVFGVFV
IAAIGGMISL VPGGFGSFDL LFLLGMEQLG YHQEAIVTSI VLYRLAYSFI PFILGLFFAA
GDLTENTMKR LETNPRIAPA IETTNVLLVV QRAVLVRILQ GSLSLIVFVA GLIVLASVSL
PIDRLTVIPH IPRPALLLFN GLSLSSALIL LILPIELYKR TKRSYTMAIT ALVGGFVFSF
LKGLNISAIF VLPMIIVLLV LLKKQFVREQ ASYTLGQLIF AVALFTVALF NYNLIAGFIW
DRMKKVLRHE YFVHSTSHIT HATIMAIIIV PLFFLIFTVV YHKRTKPIGE KADPERLAAF
LNEKGGNALS HLGFLGDKRF YFSSDGNALL LFGKIARRLV VLGDPSGQRE SFPLVLEEFL
NEAHQKGFSV LFYQIEREDM ALYHDFGYNF FKLGEEAYVD LNTFTLTGKK KAGLRAINNR
FEREEYTFHV DHPPFSDAFL EELKQISDEW LGSKKEKGFS LGFFDPSYLQ KAPIAYMKNA
EGEIVAFANV MPMYQEGEIS VDLMRYRGDA PNGIMDALFI RMFLWAKEEG CTSFNMGMAP
LANVGTAFTS FWSERFAAVI FNNVRYMYSF SGLRAFKEKY KPEWRGKYLA YRKNRSLSVT
MFLVTRLIGK SKKDSV
