LRGB_BACSU
ID LRGB_BACSU Reviewed; 231 AA.
AC P94516;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Antiholin-like protein LrgB {ECO:0000255|HAMAP-Rule:MF_01142};
GN Name=lrgB {ECO:0000255|HAMAP-Rule:MF_01142}; Synonyms=ysbB;
GN OrderedLocusNames=BSU28900;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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; Z75208; CAA99613.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14850.1; -; Genomic_DNA.
DR PIR; D69983; D69983.
DR RefSeq; NP_390768.1; NC_000964.3.
DR RefSeq; WP_003229482.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P94516; -.
DR STRING; 224308.BSU28900; -.
DR TCDB; 2.A.122.1.6; the lrgb/cidb holin-like glycolate/glycerate transporter (lrgb/cidb/ggt) family.
DR PaxDb; P94516; -.
DR PRIDE; P94516; -.
DR EnsemblBacteria; CAB14850; CAB14850; BSU_28900.
DR GeneID; 937418; -.
DR KEGG; bsu:BSU28900; -.
DR PATRIC; fig|224308.179.peg.3138; -.
DR eggNOG; COG1346; Bacteria.
DR InParanoid; P94516; -.
DR OMA; PLHTAYA; -.
DR PhylomeDB; P94516; -.
DR BioCyc; BSUB:BSU28900-MON; -.
DR Proteomes; UP000001570; 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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..231
FT /note="Antiholin-like protein LrgB"
FT /id="PRO_0000217055"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 91..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 149..171
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
FT TRANSMEM 207..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01142"
SQ SEQUENCE 231 AA; 24397 MW; 4278DD4571D08FD7 CRC64;
MESTMSPYFG IVVSLAAFGI GTFLFKKTKG FFLFTPLFVA MVLGIAFLKI GGFSYADYNN
GGEIIKFFLE PATIAFAIPL YKQRDKLKKY WWQIMASIIA GSICSVTIVY LLAKGIHLDS
AVMKSMLPQA ATTAIALPLS KGIGGISDIT AFAVIFNAVI VYALGALFLK VFKVKNPISK
GLALGTSGHA LGVAVGIEMG EVEAAMASIA VVVVGVVTVL VIPVFVQLIG G
