LRGB_STAA8
ID LRGB_STAA8 Reviewed; 233 AA.
AC P60643; P72359; Q2G1B2;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Antiholin-like protein LrgB;
GN Name=lrgB; OrderedLocusNames=SAOUHSC_00233;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REGULATION BY LYTR/LYTS.
RX PubMed=8824633; DOI=10.1128/jb.178.19.5810-5812.1996;
RA Brunskill E.W., Bayles K.W.;
RT "Identification of LytSR-regulated genes from Staphylococcus aureus.";
RL J. Bacteriol. 178:5810-5812(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP FUNCTION.
RX PubMed=10714982; DOI=10.1128/jb.182.7.1794-1801.2000;
RA Groicher K.H., Firek B.A., Fujimoto D.F., Bayles K.W.;
RT "The Staphylococcus aureus lrgAB operon modulates murein hydrolase activity
RT and penicillin tolerance.";
RL J. Bacteriol. 182:1794-1801(2000).
RN [4]
RP INTERACTION WITH CIDAB.
RX PubMed=12670989; DOI=10.1128/jb.185.8.2635-2643.2003;
RA Rice K.C., Firek B.A., Nelson J.B., Yang S.-J., Patton T.G., Bayles K.W.;
RT "The Staphylococcus aureus cidAB operon: evaluation of its role in
RT regulation of murein hydrolase activity and penicillin tolerance.";
RL J. Bacteriol. 185:2635-2643(2003).
RN [5]
RP REVIEW.
RX PubMed=14617136; DOI=10.1046/j.1365-2958.2003.t01-1-03720.x;
RA Rice K.C., Bayles K.W.;
RT "Death's toolbox: examining the molecular components of bacterial
RT programmed cell death.";
RL Mol. Microbiol. 50:729-738(2003).
CC -!- FUNCTION: Inhibits the expression or activity of extracellular murein
CC hydrolases by interacting, possibly with LrgA, with the holin-like
CC proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the
CC proton motive force of the membrane. Increases tolerance to penicillin
CC possibly by inhibiting the formation of the CidAB holin-like complexes
CC within the membrane, thus reducing penicillin-induced lethality.
CC Possibly plays a role in programmed cell death (PCD), triggering PCD in
CC response to penicillin, and possibly other antibiotics, and
CC environmental stresses. {ECO:0000269|PubMed:10714982}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Regulated by the two-component system LytR/LytS.
CC -!- SIMILARITY: Belongs to the CidB/LrgB family. LrgB subfamily.
CC {ECO:0000305}.
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DR EMBL; U52961; AAC44840.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29408.1; -; Genomic_DNA.
DR RefSeq; WP_000607067.1; NZ_LS483365.1.
DR RefSeq; YP_498828.1; NC_007795.1.
DR AlphaFoldDB; P60643; -.
DR STRING; 1280.SAXN108_0243; -.
DR TCDB; 2.A.122.1.3; the lrgb/cidb holin-like glycolate/glycerate transporter (lrgb/cidb/ggt) family.
DR EnsemblBacteria; ABD29408; ABD29408; SAOUHSC_00233.
DR GeneID; 3920308; -.
DR KEGG; sao:SAOUHSC_00233; -.
DR PATRIC; fig|93061.5.peg.214; -.
DR eggNOG; COG1346; Bacteria.
DR HOGENOM; CLU_082099_1_0_9; -.
DR OMA; PLHTAYA; -.
DR PRO; PR:P60643; -.
DR Proteomes; UP000008816; 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:0019835; P:cytolysis; IEA:UniProtKB-UniRule.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-UniRule.
DR GO; GO:1900231; P:regulation of single-species biofilm formation on inanimate substrate; IMP:CACAO.
DR HAMAP; MF_01142; LrgB; 1.
DR InterPro; IPR024891; Antiholin-like_LrgB.
DR InterPro; IPR007300; CidB/LrgB.
DR PANTHER; PTHR30249; PTHR30249; 1.
DR Pfam; PF04172; LrgB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytolysis; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..233
FT /note="Antiholin-like protein LrgB"
FT /id="PRO_0000217061"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..232
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 233 AA; 25097 MW; 089E84B7C8246C4E CRC64;
MINHLALNTP YFGILLSVIP FFLATILFEK TNRFFLFAPL FVSMVFGVAF LYLTGIPYKT
YKIGGDIIYF FLEPATICFA IPLYKKREVL VKHWHRIIGG IGIGTVVALL IILTFAKLAQ
FANDVILSML PQAATTAIAL PVSAGIGGIK ELTSLAVILN GVIIYALGNK FLKLFRITNP
IARGLALGTS GHTLGVAPAK ELGPVEESMA SIALVLVGVV VVAVVPVFVA IFF
