CIDA_STAEQ
ID CIDA_STAEQ Reviewed; 130 AA.
AC Q5HL70;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Holin-like protein CidA {ECO:0000255|HAMAP-Rule:MF_01143};
GN Name=cidA {ECO:0000255|HAMAP-Rule:MF_01143}; OrderedLocusNames=SERP2117;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW52994.1; -; Genomic_DNA.
DR RefSeq; WP_001832353.1; NC_002976.3.
DR AlphaFoldDB; Q5HL70; -.
DR STRING; 176279.SERP2117; -.
DR EnsemblBacteria; AAW52994; AAW52994; SERP2117.
DR GeneID; 50017813; -.
DR KEGG; ser:SERP2117; -.
DR eggNOG; COG1380; Bacteria.
DR HOGENOM; CLU_113736_2_1_9; -.
DR OMA; MSVMFIP; -.
DR OrthoDB; 1846131at2; -.
DR Proteomes; UP000000531; 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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..130
FT /note="Holin-like protein CidA"
FT /id="PRO_0000213186"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
FT TRANSMEM 31..51
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 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01143"
SQ SEQUENCE 130 AA; 14514 MW; 80126F879D853E4E CRC64;
MEKAKFVIKL ILQLALIMLI TFIGTEVQKL LHIPLAGSIV GLMLFFLLLQ FKIVPESWIN
VGADFLLKTM VFFFIPSVVG IMDVASNITM NYILFFIVII IGTCLVALSS GYIAEKMLEK
SNTRKGTDHS