ID   CIDA_STAA9              Reviewed;         131 AA.
AC   A5IVW8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Holin-like protein CidA {ECO:0000255|HAMAP-Rule:MF_01143};
GN   Name=cidA {ECO:0000255|HAMAP-Rule:MF_01143};
GN   OrderedLocusNames=SaurJH9_2564;
OS   Staphylococcus aureus (strain JH9).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=359786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JH9;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT   JH9.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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 CidAB proteins. When a
CC       cell is stressed by the addition of antibiotics or by other factors in
CC       the environment, the CidAB proteins possibly oligomerize within the
CC       bacterial cell membrane, creating lesions that disrupt the proton
CC       motive force, which in turn results in loss of cell viability. These
CC       lesions are also hypothesized to regulate the subsequent cell lysis by
CC       either allowing the murein hydrolases access to the cell wall substrate
CC       and/or regulating their activity by a possible change in the cell wall
CC       pH that 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; CP000703; ABQ50341.1; -; Genomic_DNA.
DR   RefSeq; WP_000549734.1; NC_009487.1.
DR   AlphaFoldDB; A5IVW8; -.
DR   KEGG; saj:SaurJH9_2564; -.
DR   HOGENOM; CLU_113736_2_1_9; -.
DR   OMA; MSVMFIP; -.
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..131
FT                   /note="Holin-like protein CidA"
FT                   /id="PRO_1000085038"
FT   TRANSMEM        4..24
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        65..85
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   131 AA;  14730 MW;  7AD5592F81678A0E CRC64;
     MHKVQLIIKL LLQLGIIIVI TYIGTEIQKI FHLPLAGSIV GLFLFYLLLQ FKIVPLTWVE
     DGANFLLKTM VFFFIPSVVG IMDVASEITL NYILFFAVII IGTCIVALSS GYIAEKMSVK
     HKHRKGVDAY E