ID   CIDA_BACSU              Reviewed;         128 AA.
AC   P39591;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Holin-like protein CidA {ECO:0000255|HAMAP-Rule:MF_01143};
GN   Name=cidA {ECO:0000255|HAMAP-Rule:MF_01143}; Synonyms=ywbH;
GN   OrderedLocusNames=BSU38320; ORFNames=ipa-23r;
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=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
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: Increases the activity of extracellular murein hydrolases
CC       possibly by mediating their export via hole formation. Inhibited by the
CC       antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB
CC       products probably inhibit the function of the CidA protein. When a cell
CC       is stressed by the addition of antibiotics or by other factors in the
CC       environment, CidA possibly oligomerizes within the bacterial cell
CC       membrane, creating lesions that disrupt the proton motive force, which
CC       in turn results in loss of cell viability. These lesions are also
CC       hypothesized to regulate the subsequent cell lysis by either allowing
CC       the murein hydrolases access to the cell wall substrate and/or
CC       regulating their activity by a possible change in the cell wall pH that
CC       results from loss of membrane potential. {ECO:0000255|HAMAP-
CC       Rule:MF_01143}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01143};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01143}.
CC   -!- SIMILARITY: Belongs to the CidA/LrgA family. CidA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01143}.
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DR   EMBL; X73124; CAA51579.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15858.1; -; Genomic_DNA.
DR   PIR; S39678; S39678.
DR   RefSeq; NP_391711.1; NC_000964.3.
DR   RefSeq; WP_003227375.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P39591; -.
DR   SMR; P39591; -.
DR   STRING; 224308.BSU38320; -.
DR   TCDB; 1.E.14.1.16; the cida/lrga holin (cida/lrga holin) family.
DR   PaxDb; P39591; -.
DR   PRIDE; P39591; -.
DR   EnsemblBacteria; CAB15858; CAB15858; BSU_38320.
DR   GeneID; 937321; -.
DR   KEGG; bsu:BSU38320; -.
DR   PATRIC; fig|224308.179.peg.4148; -.
DR   eggNOG; COG1380; Bacteria.
DR   InParanoid; P39591; -.
DR   OMA; NWVRAGA; -.
DR   BioCyc; BSUB:BSU38320-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_01143; CidA; 1.
DR   InterPro; IPR023760; Holin-like_CidA.
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..128
FT                   /note="Holin-like protein CidA"
FT                   /id="PRO_0000213177"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
SQ   SEQUENCE   128 AA;  14261 MW;  9A2FD7A0D493D13A CRC64;
     MKKLLLTVIQ IALLFIFARL INWVTALLHI NIPGSIIGIV ILFTLLHFNI IKLEWIELGA
     AWLLGELLLF FIPSAVGVIE YGDIMSKFGV SILLVVIIST FVVMVSTGTL TQLIAKRKEK
     KHTCSSEL