ID   CIDA_BACC1              Reviewed;         121 AA.
AC   Q733F5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Holin-like protein CidA {ECO:0000255|HAMAP-Rule:MF_01143};
GN   Name=cidA {ECO:0000255|HAMAP-Rule:MF_01143}; OrderedLocusNames=BCE_3703;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS42608.1; -; Genomic_DNA.
DR   RefSeq; WP_000872364.1; NC_003909.8.
DR   AlphaFoldDB; Q733F5; -.
DR   SMR; Q733F5; -.
DR   EnsemblBacteria; AAS42608; AAS42608; BCE_3703.
DR   GeneID; 59155828; -.
DR   GeneID; 64202218; -.
DR   KEGG; bca:BCE_3703; -.
DR   HOGENOM; CLU_113736_3_2_9; -.
DR   OMA; NWVRAGA; -.
DR   Proteomes; UP000002527; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..121
FT                   /note="Holin-like protein CidA"
FT                   /id="PRO_1000065446"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
SQ   SEQUENCE   121 AA;  13735 MW;  0E9AC52D988A81F2 CRC64;
     MKWWKLSGQI LLLFCFAWTG EWIAKQAHLP VPGSIIGIFL LLISLKFNLV KKEWIQDGAD
     FLLKELILFF IPSAVAVIRY KDTLSQYGID LILIIMISTL CVTLVTGLLT ELLLKRKGSV
     Q