ID   TRAP_STAEQ              Reviewed;         167 AA.
AC   Q5HNA3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Signal transduction protein TRAP;
DE   AltName: Full=Target of RNAIII-activating protein;
GN   Name=traP; OrderedLocusNames=SERP1369;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND EXPRESSION.
RX   PubMed=16842355; DOI=10.1111/j.1574-6968.2006.00327.x;
RA   Yang X.-M., Li N., Chen J.-M., Ou Y.-Z., Jin H., Lu H.-J., Zhu Y.-L.,
RA   Qin Z.-Q., Qu D., Yang P.-Y.;
RT   "Comparative proteomic analysis between the invasive and commensal strains
RT   of Staphylococcus epidermidis.";
RL   FEMS Microbiol. Lett. 261:32-40(2006).
CC   -!- FUNCTION: Contributes to virulence and biofilm formation.
CC       {ECO:0000269|PubMed:16842355}.
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. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Up-expressed in ATCC 35984 compared with ATCC 12228.
CC   -!- SIMILARITY: Belongs to the TRAP family. {ECO:0000305}.
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DR   EMBL; CP000029; AAW54746.1; -; Genomic_DNA.
DR   RefSeq; WP_001829811.1; NC_002976.3.
DR   AlphaFoldDB; Q5HNA3; -.
DR   SMR; Q5HNA3; -.
DR   STRING; 176279.SERP1369; -.
DR   EnsemblBacteria; AAW54746; AAW54746; SERP1369.
DR   GeneID; 50018411; -.
DR   KEGG; ser:SERP1369; -.
DR   eggNOG; COG2329; Bacteria.
DR   HOGENOM; CLU_116220_0_0_9; -.
DR   OMA; YFGFANR; -.
DR   OrthoDB; 1626725at2; -.
DR   Proteomes; UP000000531; 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   Membrane; Phosphoprotein; Reference proteome; Virulence.
FT   CHAIN           1..167
FT                   /note="Signal transduction protein TRAP"
FT                   /id="PRO_0000289347"
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