CIDA_BACCZ
ID CIDA_BACCZ Reviewed; 121 AA.
AC Q637F8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Holin-like protein CidA {ECO:0000255|HAMAP-Rule:MF_01143};
GN Name=cidA {ECO:0000255|HAMAP-Rule:MF_01143}; OrderedLocusNames=BCE33L3375;
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU16889.1; -; Genomic_DNA.
DR RefSeq; WP_000872364.1; NZ_CP009968.1.
DR AlphaFoldDB; Q637F8; -.
DR SMR; Q637F8; -.
DR EnsemblBacteria; AAU16889; AAU16889; BCE33L3375.
DR GeneID; 59155828; -.
DR GeneID; 64202218; -.
DR KEGG; bcz:BCE33L3375; -.
DR PATRIC; fig|288681.22.peg.2043; -.
DR OMA; NWVRAGA; -.
DR Proteomes; UP000002612; 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..121
FT /note="Holin-like protein CidA"
FT /id="PRO_1000065447"
FT TRANSMEM 3..23
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 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
SQ SEQUENCE 121 AA; 13735 MW; 0E9AC52D988A81F2 CRC64;
MKWWKLSGQI LLLFCFAWTG EWIAKQAHLP VPGSIIGIFL LLISLKFNLV KKEWIQDGAD
FLLKELILFF IPSAVAVIRY KDTLSQYGID LILIIMISTL CVTLVTGLLT ELLLKRKGSV
Q