ID   LRGA_STAES              Reviewed;         152 AA.
AC   Q8CN54;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Antiholin-like protein LrgA {ECO:0000255|HAMAP-Rule:MF_01141};
GN   Name=lrgA {ECO:0000255|HAMAP-Rule:MF_01141}; OrderedLocusNames=SE_2013;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Inhibits the expression or activity of extracellular murein
CC       hydrolases by interacting, possibly with LrgB, 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. May be involved in programmed cell
CC       death (PCD), possibly triggering PCD in response to antibiotics and
CC       environmental stresses. {ECO:0000255|HAMAP-Rule:MF_01141}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01141};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01141}.
CC   -!- SIMILARITY: Belongs to the CidA/LrgA family. LrgA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01141}.
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DR   EMBL; AE015929; AAO05654.1; -; Genomic_DNA.
DR   RefSeq; NP_765568.1; NC_004461.1.
DR   RefSeq; WP_011082790.1; NZ_WBME01000003.1.
DR   AlphaFoldDB; Q8CN54; -.
DR   SMR; Q8CN54; -.
DR   STRING; 176280.SE_2013; -.
DR   EnsemblBacteria; AAO05654; AAO05654; SE_2013.
DR   KEGG; sep:SE_2013; -.
DR   PATRIC; fig|176280.10.peg.1966; -.
DR   eggNOG; COG1380; Bacteria.
DR   HOGENOM; CLU_113736_0_1_9; -.
DR   OMA; TGWMTQL; -.
DR   Proteomes; UP000001411; 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   HAMAP; MF_01141; LrgA; 1.
DR   InterPro; IPR023736; Antiholin-like_LrgA.
DR   InterPro; IPR005538; LrgA/CidA.
DR   PANTHER; PTHR33931; PTHR33931; 1.
DR   Pfam; PF03788; LrgA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cytolysis; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..152
FT                   /note="Antiholin-like protein LrgA"
FT                   /id="PRO_0000213197"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
SQ   SEQUENCE   152 AA;  16399 MW;  CDDB57D0587EBB26 CRC64;
     MVILEQTHLV KNKAVDNKKS MKYSIFQQAL TIAVILLISK IIESFMPIPM PASVIGLVLL
     FIALCTGIVK LGQVETVGTA LTNNIGFLFV PAGISVINSL PILKQSPILI ILLIIISTLL
     LLICTGFSSQ LLVTKSLFPS KEKNEETSHI GG