ID   CIDB_STAEQ              Reviewed;         229 AA.
AC   Q5HL71;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Holin-like protein CidB;
GN   Name=cidB; OrderedLocusNames=SERP2116;
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 (By similarity).
CC       {ECO:0000250}.
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; CP000029; AAW52993.1; -; Genomic_DNA.
DR   RefSeq; WP_001832367.1; NC_002976.3.
DR   AlphaFoldDB; Q5HL71; -.
DR   STRING; 176279.SERP2116; -.
DR   EnsemblBacteria; AAW52993; AAW52993; SERP2116.
DR   GeneID; 50017814; -.
DR   KEGG; ser:SERP2116; -.
DR   eggNOG; COG1346; Bacteria.
DR   HOGENOM; CLU_082099_1_0_9; -.
DR   OMA; AQFVHFM; -.
DR   OrthoDB; 1416872at2; -.
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-KW.
DR   InterPro; IPR007300; CidB/LrgB.
DR   PANTHER; PTHR30249; PTHR30249; 1.
DR   Pfam; PF04172; LrgB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cytolysis; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..229
FT                   /note="Holin-like protein CidB"
FT                   /id="PRO_0000217052"
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..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   229 AA;  24798 MW;  216DD4FB123E05D1 CRC64;
     MNEYLQAVLM ILLTIVLYYV SKKIQDKYNN PLLNPALIAS IAIIIVLLVC GVSYKGYMKG
     GTWINHVLNA TVVCLAYPLY QNKKKIKKYL TIIFTSVLTG VVLNFVLVFT TLKIFGYSKD
     TIVTLLPRSI TAAVGIEVSQ ELGGTDTITV LFIITTGLIG SILGSMLLRM GGFKSSIARG
     LTYGNASHAF GTAKALELDI ESGAFSSIGM ILTAVISSVL IPVLILLFY