ID   CIDA2_BACCR             Reviewed;         118 AA.
AC   Q81A38;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Holin-like protein CidA 2;
GN   Name=cidA2; OrderedLocusNames=BC_3755;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CidA/LrgA family. CidA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE016877; AAP10680.1; -; Genomic_DNA.
DR   RefSeq; NP_833479.1; NC_004722.1.
DR   RefSeq; WP_000878488.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81A38; -.
DR   SMR; Q81A38; -.
DR   STRING; 226900.BC_3755; -.
DR   EnsemblBacteria; AAP10680; AAP10680; BC_3755.
DR   GeneID; 67508392; -.
DR   KEGG; bce:BC3755; -.
DR   PATRIC; fig|226900.8.peg.3870; -.
DR   HOGENOM; CLU_113736_3_2_9; -.
DR   OMA; TGLMEYG; -.
DR   Proteomes; UP000001417; 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..118
FT                   /note="Holin-like protein CidA 2"
FT                   /id="PRO_0000213176"
FT   TRANSMEM        4..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   118 AA;  13130 MW;  4DFADDEB26FBD4F1 CRC64;
     MKYVTLLLQV GVLYVFSLVG TWIQGVFHLS MPGSLIGMLI LFLLLSTRVL PLKWFELGAE
     KLIVFLPLFL IPSTTGLMEY GSFLFSKESI IFLLVVASTV VTLIVSGYIS QLLITTKK