ID   TARP_CHLTR              Reviewed;        1005 AA.
AC   O84462;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Translocated actin-recruiting phosphoprotein;
DE            Short=Tarp protein;
GN   Name=tarP; OrderedLocusNames=CT_456;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- FUNCTION: Appears to initiate or participate in signaling events that
CC       regulate the actin recruitment, which ultimately leads to
CC       internalization. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion
CC       system and translocated into host cell. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chlamydial CPn_0572/CT_456/TC_0741 family.
CC       {ECO:0000305}.
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DR   EMBL; AE001273; AAC68056.1; -; Genomic_DNA.
DR   PIR; C71513; C71513.
DR   RefSeq; NP_219969.1; NC_000117.1.
DR   RefSeq; WP_010725202.1; NC_000117.1.
DR   AlphaFoldDB; O84462; -.
DR   STRING; 272561.CT_456; -.
DR   EnsemblBacteria; AAC68056; AAC68056; CT_456.
DR   GeneID; 884231; -.
DR   KEGG; ctr:CT_456; -.
DR   PATRIC; fig|272561.5.peg.493; -.
DR   HOGENOM; CLU_011849_0_0_0; -.
DR   OMA; WRRGHQV; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042169; F:SH2 domain binding; IPI:CAFA.
DR   InterPro; IPR011443; DUF1547.
DR   Pfam; PF07577; DUF1547; 3.
PE   3: Inferred from homology;
KW   Phosphoprotein; Reference proteome; Secreted; Virulence.
FT   CHAIN           1..1005
FT                   /note="Translocated actin-recruiting phosphoprotein"
FT                   /id="PRO_0000072435"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..749
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        73..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..744
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;  102132 MW;  EC47EC389851CD1E CRC64;
     MTNSISGYQP TVTTSTSSTT SASGASGSLG ASSVSTTANA TVTQTANATN SAATSSIQTT
     GETVVNYTNS ASAPNVTVST SSSSTQATAT SNKTSQAVAG KITSPDTSES SETSSTSSSD
     HIPSDYDDVG SNSGDISNNY DDVGSNNGDI SSNYDDAAAD YEPIRTTENI YESIGGSRTS
     GPENTSGGAA AALNSLRGSS YSNYDDAAAD YEPIRTTENI YESIGGSRTS GPENTSGGAA
     AALNSLRGSS YSNYDDAAAD YEPIRTTENI YESIGGSRTS GPENTSDGAA AAALNSLRGS
     SYTTGPRNEG VFGPGPEGLP DMSLPSYDPT NKTSLLTFLS NPHVKSKMLE NSGHFVFIDT
     DRSSFILVPN GNWDQVCSIK VQNGKTKEDL DIKDLENMCA KFCTGFSKFS GDWDSLVEPM
     VSAKAGVASG GNLPNTVIIN NKFKTCVAYG PWNSQEASSG YTPSAWRRGH RVDFGGIFEK
     ANDFNKINWG TQAGPSSEDD GISFSNETPG AGPAAAPSPT PSSIPIINVN VNVGGTNVNI
     GDTNVNTTNT TPTTQSTDAS TDTSDIDDIN TNNQTDDINT TDKDSDGAGG VNGDISETES
     SSGDDSGSVS SSESDKNASV GNDGPAMKDI LSAVRKHLDV VYPGENGGST EGPLPANQTL
     GDVISDVENK GSAQDTKLSG NTGAGDDDPT TTAAVGNGAE EITLSDTDSG IGDDVSDTAS
     SSGDESGGVS SPSSESNKNT AVGNDGPSGL DILAAVRKHL DKVYPGDNGG STEGPLQANQ
     TLGDIVQDME TTGTSQETVV SPWKGSTSST ESAGGSGSVQ TLLPSPPPTP STTTLRTGTG
     ATTTSLMMGG PIKADIITTG GGGRIPGGGT LEKLLPRIRA HLDISFDAQG DLVSTEEPQL
     GSIVNKFRQE TGSRGILAFV ESAPGKPGSA QVLTGTGGDK GNLFQAAAAV TQALGNVAGK
     VNLAIQGQKL SSLVNDDGKG SVGRDLFQAA AQTTQVLSAL IDTVG