ID   TRAP_STAEP              Reviewed;         167 AA.
AC   Q8GQQ1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Signal transduction protein TRAP;
DE   AltName: Full=Target of RNAIII-activating protein;
GN   Name=traP;
OS   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Balaban N.;
RT   "TRAP, a signal transducer in Staphylococcus epidermidis.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   RIP INHIBITION OF TRAP PHOSPHORYLATION.
RC   STRAIN=Clinical isolate;
RX   PubMed=12599079; DOI=10.1086/345879;
RA   Balaban N., Giacometti A., Cirioni O., Gov Y., Ghiselli R., Mocchegiani F.,
RA   Viticchi C., Del Prete M.S., Saba V., Scalise G., Dell'Acqua G.;
RT   "Use of the quorum-sensing inhibitor RNAIII-inhibiting peptide to prevent
RT   biofilm formation in vivo by drug-resistant Staphylococcus epidermidis.";
RL   J. Infect. Dis. 187:625-630(2003).
CC   -!- FUNCTION: Contributes to virulence and biofilm formation.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane. Note=Membrane-associated.
CC       {ECO:0000250}.
CC   -!- PTM: Each of the three conserved histidine residues contributes to TRAP
CC       phosphorylation. Phosphorylation is essential for TRAP activity (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: RIP inhibits TRAP phosphorylation.
CC   -!- SIMILARITY: Belongs to the TRAP family. {ECO:0000305}.
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DR   EMBL; AF331164; AAN31185.1; -; Genomic_DNA.
DR   RefSeq; WP_001829811.1; NZ_WLVA01000001.1.
DR   AlphaFoldDB; Q8GQQ1; -.
DR   SMR; Q8GQQ1; -.
DR   GeneID; 50018411; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS51725; ABM; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Virulence.
FT   CHAIN           1..167
FT                   /note="Signal transduction protein TRAP"
FT                   /id="PRO_0000289345"
FT   DOMAIN          66..157
FT                   /note="ABM"
FT   MOD_RES         65
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         78
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         153
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   167 AA;  19529 MW;  F49D34EE4F5F9F6A CRC64;
     MYLYTSYGTY QFLNQIKLNH QERSLFQFST NDSSIILEES EGKSILKHPS SYQVIDSTGE
     FNEHHFYSAI FVPTSEDHRQ QLEKKLLHVD VPLSNFGGFK SYRLLKPTEG STYKIYFGFA
     NRTAYEDFKA SDIFNENFSK DALSQYFGAS GQHSSYFERY LYPIEDH