ID   LRGA_STAAT              Reviewed;         147 AA.
AC   A8Z0M5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Antiholin-like protein LrgA {ECO:0000255|HAMAP-Rule:MF_01141};
GN   Name=lrgA {ECO:0000255|HAMAP-Rule:MF_01141};
GN   OrderedLocusNames=USA300HOU_0273;
OS   Staphylococcus aureus (strain USA300 / TCH1516).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=451516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300 / TCH1516;
RX   PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA   Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA   Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O.,
RA   Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M.,
RA   Hemphill L., Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H.,
RA   Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V.,
RA   Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT   "Subtle genetic changes enhance virulence of methicillin resistant and
RT   sensitive Staphylococcus aureus.";
RL   BMC Microbiol. 7:99-99(2007).
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; CP000730; ABX28304.1; -; Genomic_DNA.
DR   RefSeq; WP_001792906.1; NC_010079.1.
DR   AlphaFoldDB; A8Z0M5; -.
DR   SMR; A8Z0M5; -.
DR   KEGG; sax:USA300HOU_0273; -.
DR   HOGENOM; CLU_113736_0_1_9; -.
DR   OMA; TGWMTQL; -.
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..147
FT                   /note="Antiholin-like protein LrgA"
FT                   /id="PRO_1000085031"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
SQ   SEQUENCE   147 AA;  15780 MW;  2F1015429E1F6E47 CRC64;
     MVVKQQKDAS KPAHFFHQVI VIALVLFVSK IIESFMPIPM PASVIGLVLL FVLLCTGAVK
     LGEVEKVGTT LTNNIGLLFV PAGISVVNSL GVISQAPFLI IGLIIVSTIL LLICTGYVTQ
     IIMKVTSRSK GDKVTKKIKI EEAQAHD