ID   CIDB_STAA8              Reviewed;         229 AA.
AC   P60639; Q2FV85;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Holin-like protein CidB;
GN   Name=cidB; OrderedLocusNames=SAOUHSC_02850;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH LRGAB.
RX   PubMed=12670989; DOI=10.1128/jb.185.8.2635-2643.2003;
RA   Rice K.C., Firek B.A., Nelson J.B., Yang S.-J., Patton T.G., Bayles K.W.;
RT   "The Staphylococcus aureus cidAB operon: evaluation of its role in
RT   regulation of murein hydrolase activity and penicillin tolerance.";
RL   J. Bacteriol. 185:2635-2643(2003).
RN   [3]
RP   REVIEW.
RX   PubMed=14617136; DOI=10.1046/j.1365-2958.2003.t01-1-03720.x;
RA   Rice K.C., Bayles K.W.;
RT   "Death's toolbox: examining the molecular components of bacterial
RT   programmed cell death.";
RL   Mol. Microbiol. 50:729-738(2003).
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.
CC       {ECO:0000269|PubMed:12670989}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CidB/LrgB family. CidB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD31850.1; -; Genomic_DNA.
DR   RefSeq; WP_001001019.1; NZ_LS483365.1.
DR   RefSeq; YP_501307.1; NC_007795.1.
DR   AlphaFoldDB; P60639; -.
DR   STRING; 1280.SAXN108_2789; -.
DR   EnsemblBacteria; ABD31850; ABD31850; SAOUHSC_02850.
DR   GeneID; 3921523; -.
DR   KEGG; sao:SAOUHSC_02850; -.
DR   PATRIC; fig|93061.5.peg.2578; -.
DR   eggNOG; COG1346; Bacteria.
DR   HOGENOM; CLU_082099_3_0_9; -.
DR   OMA; AQFVHFM; -.
DR   PRO; PR:P60639; -.
DR   Proteomes; UP000008816; 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-KW.
DR   InterPro; IPR007300; CidB/LrgB.
DR   PANTHER; PTHR30249; PTHR30249; 1.
DR   Pfam; PF04172; LrgB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytolysis; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..229
FT                   /note="Holin-like protein CidB"
FT                   /id="PRO_0000217049"
FT   TRANSMEM        4..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   229 AA;  25012 MW;  0A3EAF56E27C38D2 CRC64;
     MNDYVQALLM ILLTVVLYYF AKRLQQKYPN PFLNPALIAS LGIIFVLLIF GISYNGYMKG
     GSWINHILNA TVVCLAYPLY KNREKIKDNV SIIFASVLTG VMLNFMLVFL TLKAFGYSKD
     VIVTLLPRSI TAAVGIEVSH ELGGTDTMTV LFIITTGLIG SILGSMLLRF GRFESSIAKG
     LTYGNASHAF GTAKALEMDI ESGAFSSIGM ILTAVISSVL IPVLILLFY