TRAP_STAAM
ID TRAP_STAAM Reviewed; 167 AA.
AC Q7A2Q4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Signal transduction protein TRAP;
DE AltName: Full=Target of RNAIII-activating protein;
GN Name=traP; OrderedLocusNames=SAV1835;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB57997.1; -; Genomic_DNA.
DR RefSeq; WP_000737976.1; NC_002758.2.
DR AlphaFoldDB; Q7A2Q4; -.
DR SMR; Q7A2Q4; -.
DR BindingDB; Q7A2Q4; -.
DR ChEMBL; CHEMBL4105947; -.
DR World-2DPAGE; 0002:Q7A2Q4; -.
DR PaxDb; Q7A2Q4; -.
DR EnsemblBacteria; BAB57997; BAB57997; SAV1835.
DR KEGG; sav:SAV1835; -.
DR HOGENOM; CLU_116220_0_0_9; -.
DR OMA; YFGFANR; -.
DR PhylomeDB; Q7A2Q4; -.
DR BioCyc; SAUR158878:SAV_RS09900-MON; -.
DR Proteomes; UP000002481; 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_0000289340"
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; 19548 MW; 2BB731EEDBC00961 CRC64;
MKKLYTSYGT YGFLHQIKIN NPTHQLFQFS ASDTSVIFEE TDGETVLKSP SIYEVIKEIG
EFSEHHFYCA IFIPSTEDHA YQLEKKLISV DDNFRNFGGF KSYRLLRPAK GTTYKIYFGF
ADRHAYEDFK QSDAFNDHFS KDALSHYFGS SGQHSSYFER YLYPIKE