LRGA_BACSU
ID LRGA_BACSU Reviewed; 146 AA.
AC P94515;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Antiholin-like protein LrgA {ECO:0000255|HAMAP-Rule:MF_01141};
GN Name=lrgA {ECO:0000255|HAMAP-Rule:MF_01141}; Synonyms=ysbA;
GN OrderedLocusNames=BSU28910;
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 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: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; Z75208; CAA99612.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14851.1; -; Genomic_DNA.
DR PIR; C69983; C69983.
DR RefSeq; NP_390769.1; NC_000964.3.
DR RefSeq; WP_004399155.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P94515; -.
DR SMR; P94515; -.
DR STRING; 224308.BSU28910; -.
DR TCDB; 1.E.14.1.17; the cida/lrga holin (cida/lrga holin) family.
DR PaxDb; P94515; -.
DR PRIDE; P94515; -.
DR EnsemblBacteria; CAB14851; CAB14851; BSU_28910.
DR GeneID; 937417; -.
DR KEGG; bsu:BSU28910; -.
DR PATRIC; fig|224308.179.peg.3139; -.
DR eggNOG; COG1380; Bacteria.
DR InParanoid; P94515; -.
DR OMA; TGWMTQL; -.
DR BioCyc; BSUB:BSU28910-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_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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..146
FT /note="Antiholin-like protein LrgA"
FT /id="PRO_0000213189"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01141"
SQ SEQUENCE 146 AA; 15711 MW; 6B20C8C69A159AB5 CRC64;
MSAKKVYGFL TQAFIFAVIM LVSNMIAAIV PIPIPASVVG LVLLFLLLCL KVIKLEQVET
LGTSLTSLIG FLFVPSGISV MNSLGVMQQY GLQIVLVILL ATIILLGATG LFSQLILSLS
GKRKTEADMK TKTVQSPQNN NELVHH
