ID CIDA_STAA1 Reviewed; 131 AA.
AC A7X6P6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Holin-like protein CidA {ECO:0000255|HAMAP-Rule:MF_01143};
GN Name=cidA {ECO:0000255|HAMAP-Rule:MF_01143}; OrderedLocusNames=SAHV_2525;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF79408.1; -; Genomic_DNA.
DR RefSeq; WP_000549734.1; NC_009782.1.
DR AlphaFoldDB; A7X6P6; -.
DR SMR; A7X6P6; -.
DR KEGG; saw:SAHV_2525; -.
DR HOGENOM; CLU_113736_2_1_9; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-UniRule.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
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:SF2; HOLIN-LIKE PROTEIN CIDA; 1.
DR PANTHER; PTHR33931; HOLIN-LIKE PROTEIN CIDA-RELATED; 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_1000065450"
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
//
