ID C3GBD7_BACTU Unreviewed; 146 AA.
AC C3GBD7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Antiholin-like protein LrgA {ECO:0000256|HAMAP-Rule:MF_01141};
GN Name=lrgA {ECO:0000256|HAMAP-Rule:MF_01141};
GN ORFNames=bthur0009_51570 {ECO:0000313|EMBL:EEM68772.1};
OS Bacillus thuringiensis serovar andalousiensis BGSC 4AW1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM68772.1};
RN [1] {ECO:0000313|EMBL:EEM68772.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM68772.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
CC -!- FUNCTION: Inhibits the expression or activity of extracellular murein
CC hydrolases by interacting, possibly with LrgB, with the holin-like
CC protein CidA. The LrgAB and CidA proteins may affect the proton motive
CC force of the membrane. May be involved in programmed cell death (PCD),
CC possibly triggering PCD in response to antibiotics and environmental
CC stresses. {ECO:0000256|HAMAP-Rule:MF_01141}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01141};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CidA/LrgA family. LrgA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEM68772.1}.
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DR EMBL; ACNG01000119; EEM68772.1; -; Genomic_DNA.
DR AlphaFoldDB; C3GBD7; -.
DR HOGENOM; CLU_113736_0_1_9; -.
DR Proteomes; UP000001380; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-UniRule.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
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:SF4; ANTIHOLIN-LIKE PROTEIN LRGA; 1.
DR PANTHER; PTHR33931; HOLIN-LIKE PROTEIN CIDA-RELATED; 1.
DR Pfam; PF03788; LrgA; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01141}; Cytolysis {ECO:0000256|HAMAP-Rule:MF_01141};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01141};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01141};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01141}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01141"
FT TRANSMEM 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01141"
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01141"
FT TRANSMEM 93..116
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01141"
SQ SEQUENCE 146 AA; 15754 MW; 7E1BE587D49444DD CRC64;
MAKMSTKKVY SFLSQAFIFS AIMLISNIIA THLPIPMPSS VIGLVILFSL LCLKVIKLEQ
VESLGTALTG IIGFLFVPSG ISVINSLGVM GQYFVQILTV IVVATVILLA VTGLFAQFIL
GKDEKETEDT KELKVVNKGR KHGKVA
//
