CIDB_STAAR
ID CIDB_STAAR Reviewed; 229 AA.
AC Q6GDQ8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Holin-like protein CidB;
GN Name=cidB; OrderedLocusNames=SAR2620;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG41599.1; -; Genomic_DNA.
DR RefSeq; WP_001001018.1; NC_002952.2.
DR AlphaFoldDB; Q6GDQ8; -.
DR KEGG; sar:SAR2620; -.
DR HOGENOM; CLU_082099_3_0_9; -.
DR OMA; AQFVHFM; -.
DR OrthoDB; 1416872at2; -.
DR Proteomes; UP000000596; 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; Transmembrane; Transmembrane helix.
FT CHAIN 1..229
FT /note="Holin-like protein CidB"
FT /id="PRO_0000217047"
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; 25012 MW; 0A3EAF51927C38D2 CRC64;
MNDYVQALLM ILLTVVLYYF AKRLQQKYPN PFLNPALIAS LGIIFVLLIF GISYNGYMKG
GSWINHILNA TVVCLAYPLY KNREKIKDNV SIIFASVLTG VMLNFMLVFL TLKAFGYSKD
VIVTLLPRSI TAAVGIEVSH ELGGTDTMTV LFIITTGLIG SILGSMLLRF GRFESSIAKG
LTYGNASHAF GTAKALEMDI ESGAFSSIGM ILTAVISSVL IPVLIILFY