ID J8YJ04_BACCE Unreviewed; 121 AA.
AC J8YJ04;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Holin-like protein CidA {ECO:0000256|HAMAP-Rule:MF_01143};
GN Name=cidA {ECO:0000256|HAMAP-Rule:MF_01143};
GN ORFNames=IG3_03167 {ECO:0000313|EMBL:EJV82518.1};
OS Bacillus cereus HuA2-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053201 {ECO:0000313|EMBL:EJV82518.1, ECO:0000313|Proteomes:UP000004136};
RN [1] {ECO:0000313|EMBL:EJV82518.1, ECO:0000313|Proteomes:UP000004136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HuA2-1 {ECO:0000313|EMBL:EJV82518.1,
RC ECO:0000313|Proteomes:UP000004136};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus HuA2-1.";
RL Submitted (APR-2012) 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 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:0000256|HAMAP-
CC Rule:MF_01143}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|HAMAP-Rule:MF_01143}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-Rule:MF_01143}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CidA/LrgA family. CidA subfamily.
CC {ECO:0000256|ARBA:ARBA00010166, ECO:0000256|HAMAP-Rule:MF_01143}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01143}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJV82518.1}.
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DR EMBL; AHDV01000023; EJV82518.1; -; Genomic_DNA.
DR RefSeq; WP_002137762.1; NZ_JH804672.1.
DR AlphaFoldDB; J8YJ04; -.
DR PATRIC; fig|1053201.3.peg.3242; -.
DR HOGENOM; CLU_113736_3_2_9; -.
DR OrthoDB; 3176438at2; -.
DR Proteomes; UP000004136; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01143}; Cytolysis {ECO:0000256|HAMAP-Rule:MF_01143};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01143};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01143};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01143}.
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01143"
FT TRANSMEM 61..80
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01143"
FT TRANSMEM 92..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01143"
SQ SEQUENCE 121 AA; 13735 MW; 17609EEF66AB95B7 CRC64;
MKWWKLSGQI LLLFCFAWTG EWIAKQTHLP VPGSIIGIFL LLISLKFNIV KKEWIQDGAD
FLLKELILFF IPSAVAVIRY KDTLSQYGID LILIIVISTL CVTLVTGLLT ELLLKRKGST
Q
//
