ID   TRAP_STAAB              Reviewed;         167 AA.
AC   Q2YU04;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Signal transduction protein TRAP;
DE   AltName: Full=Target of RNAIII-activating protein;
GN   Name=traP; OrderedLocusNames=SAB1766;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: Signal transduction protein, which is a major regulator of
CC       staphylococcal pathogenesis. Phosphorylated TRAP leads to the
CC       activation of agr system and consequent RNAIII synthesis resulting in
CC       the expression of several virulence factors. Up-regulates the
CC       expression of most toxins and genes known to be necessary for biofilm
CC       formation (By similarity). {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: Phosphorylation of TRAP is activated by RAP and necessary for the
CC       induction of RNAIII gene expression but not for ongoing transcription.
CC       TRAP is dephosphorylated from the mid-exponential phase of growth,
CC       which is when agr is activated and AIP is produced. RIP acts by
CC       inhibiting TRAP phosphorylation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAP family. {ECO:0000305}.
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DR   EMBL; AJ938182; CAI81455.1; -; Genomic_DNA.
DR   RefSeq; WP_000737983.1; NC_007622.1.
DR   AlphaFoldDB; Q2YU04; -.
DR   SMR; Q2YU04; -.
DR   KEGG; sab:SAB1766; -.
DR   HOGENOM; CLU_116220_0_0_9; -.
DR   OMA; YFGFANR; -.
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   3: Inferred from homology;
KW   Membrane; Phosphoprotein; Virulence.
FT   CHAIN           1..167
FT                   /note="Signal transduction protein TRAP"
FT                   /id="PRO_0000289336"
FT   DOMAIN          67..158
FT                   /note="ABM"
FT   MOD_RES         66
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         79
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         154
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   167 AA;  19601 MW;  F9D9841594CB0B1B CRC64;
     MKKLYTSYGT YGFLNQIKIN NPSHHLFQFS TADSSVIFEE TEENTVLKSP SIYEVIKEIG
     AFNEDHFYCA IFIPSTEDHV YQLEKKLISV DDNFKNFGGF KSYRLLRPVK GTTYKIYFGF
     ADRQTYEDFK NSDAFKDHFS KEALSHYFGS SGQHSSYFER YLYPIKE