ID   TRAP_STAAW              Reviewed;         167 AA.
AC   Q8NVW1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Signal transduction protein TRAP;
DE   AltName: Full=Target of RNAIII-activating protein;
GN   Name=traP; OrderedLocusNames=MW1775;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB95640.1; -; Genomic_DNA.
DR   RefSeq; WP_000737978.1; NC_003923.1.
DR   AlphaFoldDB; Q8NVW1; -.
DR   SMR; Q8NVW1; -.
DR   EnsemblBacteria; BAB95640; BAB95640; BAB95640.
DR   KEGG; sam:MW1775; -.
DR   HOGENOM; CLU_116220_0_0_9; -.
DR   OMA; YFGFANR; -.
DR   Proteomes; UP000000418; Chromosome.
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_0000289341"
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;  19563 MW;  9BB5F1F2E1755960 CRC64;
     MKKLYTSYGT YGFLHQIKIN NPTHQLFQFS ASDTSVIFEE TDGETVLKSP TKYDVIKEIG
     EFSEHHFYCA IFIPSTEDHA YQLEKKLISV DDNFRNFGGF KSYRLLRPAK GTTYKIYFGF
     ADRHAYEDFK QSDAFNDHFS KDALSHYFGS SGQHSSYFER YLYPIKE