TARP_CHLT2
ID TARP_CHLT2 Reviewed; 1005 AA.
AC Q6GX35; B0B829;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Translocated actin-recruiting phosphoprotein;
DE Short=Tarp protein;
GN Name=tarP; OrderedLocusNames=CTL0716;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=15199184; DOI=10.1073/pnas.0402829101;
RA Clifton D.R., Fields K.A., Grieshaber S.S., Dooley C.A., Fischer E.R.,
RA Mead D.J., Carabeo R.A., Hackstadt T.;
RT "A chlamydial type III translocated protein is tyrosine-phosphorylated at
RT the site of entry and associated with recruitment of actin.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10166-10171(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
CC -!- FUNCTION: Appears to initiate or participate in signaling events that
CC regulate the actin recruitment, which ultimately leads to
CC internalization. {ECO:0000269|PubMed:15199184}.
CC -!- INTERACTION:
CC Q6GX35; P68135: ACTA1; Xeno; NbExp=4; IntAct=EBI-15605056, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion
CC system and translocated into host cell.
CC -!- PTM: Phosphorylated on a tyrosine on attachment to the host cell.
CC Tyrosine phosphorylation is temporally and spatially associated with
CC recruitment of actin to the site of chlamydial entry. Phosphorylated
CC Tarp seems to remain cytoplasmically exposed on the inclusion membrane
CC at one side of internalized elementary bodies for several hours after
CC entry.
CC -!- MISCELLANEOUS: Transcribed from mid to late cycle in the chlamydial
CC developmental cycle.
CC -!- SIMILARITY: Belongs to the chlamydial CPn_0572/CT_456/TC_0741 family.
CC {ECO:0000305}.
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DR EMBL; AY623902; AAT47185.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP04155.1; -; Genomic_DNA.
DR RefSeq; WP_009873825.1; NC_010287.1.
DR RefSeq; YP_001654788.1; NC_010287.1.
DR AlphaFoldDB; Q6GX35; -.
DR PCDDB; Q6GX35; -.
DR DIP; DIP-61288N; -.
DR IntAct; Q6GX35; 1.
DR EnsemblBacteria; CAP04155; CAP04155; CTL0716.
DR KEGG; ctb:CTL0716; -.
DR PATRIC; fig|471472.4.peg.768; -.
DR HOGENOM; CLU_011849_0_0_0; -.
DR OMA; WRRGHQV; -.
DR Proteomes; UP000000795; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051425; F:PTB domain binding; IPI:CAFA.
DR GO; GO:0042169; F:SH2 domain binding; IPI:CAFA.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:CAFA.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:CAFA.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:CAFA.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:CAFA.
DR DisProt; DP01472; -.
DR InterPro; IPR011443; DUF1547.
DR Pfam; PF07577; DUF1547; 2.
PE 1: Evidence at protein level;
KW Phosphoprotein; Secreted; Virulence.
FT CHAIN 1..1005
FT /note="Translocated actin-recruiting phosphoprotein"
FT /id="PRO_0000072436"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1005 AA; 103252 MW; 84097DC88E20F323 CRC64;
MTNSISGDQP TVTTFTSSTT SASGASGSLG ASSVSTTANA TVTQTANATN SAATSSIQTT
GETVVNYTNS ASAPTVTVST SSSSTQATAT SNKTSQAVAG KITSPDTSES SETSSTSSSD
HIPSDYEPIS TTENIYENIY ESIDDSSTSG PENTSGGAAA LNSLRGSSYS NYDDAAADYE
PISTTENIYE SIDDSSTSDP ENTSGGAAAL NSLRGSSYSN YDDAAADYEP ISTTENIYEN
IYESIDDSST SGPENTSGGA AALNSLRGSS YSNYDDAAAD YEPISTTENI YESIDDSSTS
DPENTSGGAA AALNSLRGSS YSNYDDAAAD YEPISTTENI YESIDDSSTS DPENTSGGAA
ALNSLRGSSY SNYDDAAADY EPISTTENIY ENIYESIDGS STSDPENTSG GAAAALNSLR
GSSYTTGPRN EGVFGPGPEG LPDMSLPSYD PTNKTSLLTF LSNPHVKSKM LENSGHFVFI
DTDRSSFILV PNGNWDQVCS IKVQNGKTKE DLDIKDLENM CAKFCTGFNK FSGDWDSRVE
PMMSAKAGVA SGGNLPNTVI INNKFKTCVA YGPWNSREAS SGYTPSAWRR GHQVNFGEIF
EKANDFNKIN WGTQAGPSSE DDGISFSNET PGAGPAAAPS PTPSSIPVIN VNVNVGGTNV
NIRDTNVNTT NTTPTTQSTD ASTDTSDIDN INTNNQTDDI NTTDKDSDGA GGVNGDISET
ESSSGDDSGS VSSSESDKNA SVGNDGPAMK DILSAVRKHL DVVYPGDNGG STEGPLQANQ
TLGDIVQDME TTGTSQETVV SPWKGSTSST GSAGGSGSVQ TLLPSPPPTP STTTLRTGTG
ATTTSLMMGG PIKADIITTG GGGRIPGGGT LEKLLPRIRA HLDISFDGQG DLVSTEEPQL
GSIVNKFRKE TGSGGIVASV ESAPGKPGSA QVLTGTGGDK GNLFQAAAAV TQALGNVAGK
VNLAIQGQKL SSLVNDDGKG SVGRDLFQAA TQTTQALSSL IDTVG
