ICAR_STAEQ
ID ICAR_STAEQ Reviewed; 185 AA.
AC Q5HKQ1; O70020;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Biofilm operon icaADBC HTH-type negative transcriptional regulator IcaR;
DE AltName: Full=Intercellular adhesion protein R;
GN Name=icaR; OrderedLocusNames=SERP2292;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8809760; DOI=10.1111/j.1365-2958.1996.tb02548.x;
RA Heilmann C., Schweitzer O., Gerke C., Vanittanakom N., Mack D., Goetz F.;
RT "Molecular basis of intercellular adhesion in the biofilm-forming
RT Staphylococcus epidermidis.";
RL Mol. Microbiol. 20:1083-1091(1996).
RN [2]
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).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12142410; DOI=10.1128/jb.184.16.4400-4408.2002;
RA Conlon K.M., Humphreys H., O'Gara J.P.;
RT "icaR encodes a transcriptional repressor involved in environmental
RT regulation of ica operon expression and biofilm formation in Staphylococcus
RT epidermidis.";
RL J. Bacteriol. 184:4400-4408(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS), DNA-BINDING, SUBUNIT, MUTAGENESIS
RP OF LEU-23; LYS-33 AND ALA-35, AND EFFECTS OF ANTIBIOTICS.
RX PubMed=18208836; DOI=10.1093/nar/gkm1176;
RA Jeng W.Y., Ko T.P., Liu C.I., Guo R.T., Liu C.L., Shr H.L., Wang A.H.;
RT "Crystal structure of IcaR, a repressor of the TetR family implicated in
RT biofilm formation in Staphylococcus epidermidis.";
RL Nucleic Acids Res. 36:1567-1577(2008).
CC -!- FUNCTION: Represses transcription of the icaADBC operon necessary for
CC biofilm production. {ECO:0000269|PubMed:12142410}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18208836}.
CC -!- INDUCTION: Repressed by ethanol. {ECO:0000269|PubMed:12142410}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a 5.8-fold
CC increase in ica operon expression. {ECO:0000269|PubMed:12142410}.
CC -!- MISCELLANEOUS: Binding to the ica operator DNA involves two IcaR dimers
CC and is highly cooperative. Two aminoglycoside antibiotics, namely,
CC gentamicin and streptomycin, show an inhibitory effect on the IcaR-DNA
CC interactions. Consequently, by interfering with the binding of IcaR to
CC DNA, aminoglycoside gentamicin and other antibiotics may activate the
CC icaADBC genes and elicit biofilm production in S.epidermidis, as a
CC defense mechanism. The four antibiotics kanamycin, tetracycline,
CC ampicillin and chloramphenicol do not show significant effect on the
CC IcaR-DNA binding.
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DR EMBL; U43366; AAC06121.1; -; Genomic_DNA.
DR EMBL; CP000029; AAW53174.1; -; Genomic_DNA.
DR RefSeq; WP_002497698.1; NC_002976.3.
DR PDB; 2ZCM; X-ray; 1.33 A; A/B=1-185.
DR PDB; 2ZCN; X-ray; 1.90 A; A/B/C/D=1-185.
DR PDBsum; 2ZCM; -.
DR PDBsum; 2ZCN; -.
DR AlphaFoldDB; Q5HKQ1; -.
DR SMR; Q5HKQ1; -.
DR STRING; 176279.SERP2292; -.
DR EnsemblBacteria; AAW53174; AAW53174; SERP2292.
DR KEGG; ser:SERP2292; -.
DR eggNOG; COG1309; Bacteria.
DR HOGENOM; CLU_124987_0_0_9; -.
DR OMA; ETNSYFA; -.
DR OrthoDB; 1437290at2; -.
DR EvolutionaryTrace; Q5HKQ1; -.
DR Proteomes; UP000000531; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR041646; IcaR_C.
DR Pfam; PF18665; TetR_C_37; 1.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..185
FT /note="Biofilm operon icaADBC HTH-type negative
FT transcriptional regulator IcaR"
FT /id="PRO_0000070604"
FT DOMAIN 1..59
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 22..41
FT /note="H-T-H motif"
FT /evidence="ECO:0000305"
FT MUTAGEN 23
FT /note="L->T: One-third decrease in DNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:18208836"
FT MUTAGEN 23
FT /note="L->V: 6-fold increase in DNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:18208836"
FT MUTAGEN 33
FT /note="K->E: No DNA-binding and loss of repressor
FT activity."
FT /evidence="ECO:0000269|PubMed:18208836"
FT MUTAGEN 33
FT /note="K->S: 5-fold decrease in DNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:18208836"
FT MUTAGEN 35
FT /note="A->G: 2-fold increase in DNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:18208836"
FT MUTAGEN 35
FT /note="A->P: 5-fold increase in DNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:18208836"
FT HELIX 2..16
FT /evidence="ECO:0007829|PDB:2ZCM"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 44..62
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 106..127
FT /evidence="ECO:0007829|PDB:2ZCM"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2ZCM"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 137..161
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2ZCM"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:2ZCM"
SQ SEQUENCE 185 AA; 22169 MW; CC0DCA4F68C59421 CRC64;
MKDKIIDNAI TLFSEKGYDG TTLDDISKSV NIKKASLYYH YDNKEEIYRK SVENCFNYFI
DFLLRNHDDN YSIDGLYQFL FKFIFDVDER YIKLYVQLSS APEALNSEIK HHLQEINTTL
HDELIKYYDP THIALDKEDF INLILLFLET WYFRASFSQK FGIIEDSKNR FKDQVYSLLN
VFLKK
