ID   CIDA_BACVZ              Reviewed;         128 AA.
AC   A7ZA61;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Holin-like protein CidA {ECO:0000255|HAMAP-Rule:MF_01143};
GN   Name=cidA {ECO:0000255|HAMAP-Rule:MF_01143}; OrderedLocusNames=RBAM_035580;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS75887.1; -; Genomic_DNA.
DR   RefSeq; WP_007407725.1; NC_009725.2.
DR   AlphaFoldDB; A7ZA61; -.
DR   STRING; 326423.RBAM_035580; -.
DR   EnsemblBacteria; ABS75887; ABS75887; RBAM_035580.
DR   GeneID; 66323868; -.
DR   KEGG; bay:RBAM_035580; -.
DR   HOGENOM; CLU_113736_3_2_9; -.
DR   OMA; NWVRAGA; -.
DR   Proteomes; UP000001120; 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..128
FT                   /note="Holin-like protein CidA"
FT                   /id="PRO_1000065445"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
FT   TRANSMEM        27..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;  14184 MW;  1EFB16803B2993EA CRC64;
     MKKLLLTVIQ IALLFIFARL INWVTAALHI NIPGSIIGIV ILFTLLHFKI IKLEWIELGA
     AWLLGELLLF FIPSAVGVIE YGDIMSKFGV SILLVVVIST FVVMVSTGTL TQLIAKRKEK
     KQTCSSES