LRGB_BACCN
ID LRGB_BACCN Reviewed; 230 AA.
AC A7GVI2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Antiholin-like protein LrgB {ECO:0000255|HAMAP-Rule:MF_01142};
GN Name=lrgB {ECO:0000255|HAMAP-Rule:MF_01142}; OrderedLocusNames=Bcer98_3956;
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- FUNCTION: Inhibits the expression or activity of extracellular murein
CC hydrolases by interacting, possibly with LrgA, 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:0000255|HAMAP-Rule:MF_01142}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01142};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01142}.
CC -!- SIMILARITY: Belongs to the CidB/LrgB family. LrgB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01142}.
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DR EMBL; CP000764; ABS24140.1; -; Genomic_DNA.
DR RefSeq; WP_012096403.1; NC_009674.1.
DR AlphaFoldDB; A7GVI2; -.
DR STRING; 315749.Bcer98_3956; -.
DR EnsemblBacteria; ABS24140; ABS24140; Bcer98_3956.
DR GeneID; 56419504; -.
DR KEGG; bcy:Bcer98_3956; -.
DR eggNOG; COG1346; Bacteria.
DR HOGENOM; CLU_082099_1_0_9; -.
DR OMA; PLHTAYA; -.
DR OrthoDB; 1416872at2; -.
DR Proteomes; UP000002300; 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_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 3: Inferred from homology;
KW Cell membrane; Cytolysis; Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..230
FT /note="Antiholin-like protein LrgB"
FT /id="PRO_1000085032"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
SQ SEQUENCE 230 AA; 24399 MW; C2C20979FFECCA7D CRC64;
MASTMTPYFG IVVSLIAYGI GTFLFKHSKQ FFLFTPLFVA MVLGIGFLKV GNFTFEEYNT
GGKIISFFLE PATIAFAIPL YKQADKLKKY WWQILSAIIV GSICSVVVVF IVAKAIHLDT
AIMNSMLPQA ATTAIALPLS ESIGGIPAIT SFAVIFNAVI VYALGALFLK TFRVKNPIAK
GLALGTAGHA LGVAVGIEMG EVEAAMASIA VTVVGVVTVV VIPLFMPLIA