TRAP_STAA8
ID TRAP_STAA8 Reviewed; 167 AA.
AC Q2G2F3; Q9F949;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Signal transduction protein TRAP;
DE AltName: Full=Target of RNAIII-activating protein;
GN Name=traP; OrderedLocusNames=SAOUHSC_01964;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHOSPHORYLATION, FUNCTION, AND
RP INDUCTION.
RX PubMed=11160124; DOI=10.1074/jbc.m005446200;
RA Balaban N., Goldkorn T., Gov Y., Hirshberg M., Koyfman N., Matthews H.R.,
RA Nhan R.T., Singh B., Uziel O.;
RT "Regulation of Staphylococcus aureus pathogenesis via target of RNAIII-
RT activating protein (TRAP).";
RL J. Biol. Chem. 276:2658-2667(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHOSPHORYLATION AT HIS-66; HIS-79 AND
RP HIS-154, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-66; HIS-79; HIS-124
RP AND HIS-154.
RX PubMed=14726534; DOI=10.1074/jbc.m311106200;
RA Gov Y., Borovok I., Korem M., Singh V.K., Jayaswal R.K., Wilkinson B.J.,
RA Rich S.M., Balaban N.;
RT "Quorum sensing in Staphylococci is regulated via phosphorylation of three
RT conserved histidine residues.";
RL J. Biol. Chem. 279:14665-14672(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [4]
RP FUNCTION AS A REGULATOR OF VIRULENCE FACTORS.
RX PubMed=16177293; DOI=10.1128/iai.73.10.6220-6228.2005;
RA Korem M., Gov Y., Kiran M.D., Balaban N.;
RT "Transcriptional profiling of target of RNAIII-activating protein, a master
RT regulator of staphylococcal virulence.";
RL Infect. Immun. 73:6220-6228(2005).
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. {ECO:0000269|PubMed:11160124, ECO:0000269|PubMed:16177293}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14726534}.
CC Note=Membrane-associated.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:11160124}.
CC -!- PTM: Each of the three conserved histidine residues contributes to TRAP
CC phosphorylation. Phosphorylation is essential for TRAP activity.
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.
CC -!- SIMILARITY: Belongs to the TRAP family. {ECO:0000305}.
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DR EMBL; AF202641; AAG32925.1; -; Genomic_DNA.
DR EMBL; AJ489450; CAD33705.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD31025.1; -; Genomic_DNA.
DR RefSeq; WP_000737976.1; NZ_LS483365.1.
DR RefSeq; YP_500463.1; NC_007795.1.
DR PDB; 4AE5; X-ray; 1.85 A; A/B/C/D=1-167.
DR PDBsum; 4AE5; -.
DR AlphaFoldDB; Q2G2F3; -.
DR SMR; Q2G2F3; -.
DR STRING; 1280.SAXN108_1864; -.
DR iPTMnet; Q2G2F3; -.
DR EnsemblBacteria; ABD31025; ABD31025; SAOUHSC_01964.
DR GeneID; 3920909; -.
DR KEGG; sao:SAOUHSC_01964; -.
DR PATRIC; fig|93061.5.peg.1788; -.
DR eggNOG; COG2329; Bacteria.
DR HOGENOM; CLU_116220_0_0_9; -.
DR OMA; YFGFANR; -.
DR PRO; PR:Q2G2F3; -.
DR Proteomes; UP000008816; 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 1: Evidence at protein level;
KW 3D-structure; Membrane; Phosphoprotein; Reference proteome; Virulence.
FT CHAIN 1..167
FT /note="Signal transduction protein TRAP"
FT /id="PRO_0000289343"
FT DOMAIN 67..158
FT /note="ABM"
FT MOD_RES 66
FT /note="Phosphohistidine"
FT /evidence="ECO:0000269|PubMed:14726534"
FT MOD_RES 79
FT /note="Phosphohistidine"
FT /evidence="ECO:0000269|PubMed:14726534"
FT MOD_RES 154
FT /note="Phosphohistidine"
FT /evidence="ECO:0000269|PubMed:14726534"
FT MUTAGEN 66
FT /note="H->A: Abolishes induction of RNAIII synthesis and
FT toxin production. Reduces phosphorylation."
FT /evidence="ECO:0000269|PubMed:14726534"
FT MUTAGEN 79
FT /note="H->A: Abolishes induction of RNAIII synthesis and
FT toxin production. Reduces phosphorylation."
FT /evidence="ECO:0000269|PubMed:14726534"
FT MUTAGEN 124
FT /note="H->A: No effect in induction of RNAIII synthesis and
FT toxin production."
FT /evidence="ECO:0000269|PubMed:14726534"
FT MUTAGEN 154
FT /note="H->A: Abolishes induction of RNAIII synthesis and
FT toxin production. Reduces phosphorylation."
FT /evidence="ECO:0000269|PubMed:14726534"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4AE5"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:4AE5"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4AE5"
FT STRAND 32..43
FT /evidence="ECO:0007829|PDB:4AE5"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:4AE5"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:4AE5"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:4AE5"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:4AE5"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:4AE5"
FT STRAND 100..112
FT /evidence="ECO:0007829|PDB:4AE5"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:4AE5"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:4AE5"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:4AE5"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:4AE5"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:4AE5"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:4AE5"
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
