SYCT_YEREN
ID SYCT_YEREN Reviewed; 130 AA.
AC P0C2V9; O85243; Q93KU9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Chaperone protein SycT;
GN Name=sycT;
OS Yersinia enterocolitica.
OG Plasmid pYVe227, and Plasmid pYVa127/90.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=W22703 / Serotype O:9 / Biotype 2; PLASMID=pYVe227;
RX PubMed=9723929; DOI=10.1046/j.1365-2958.1998.00992.x;
RA Iriarte M., Cornelis G.R.;
RT "YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of
RT host cells.";
RL Mol. Microbiol. 29:915-929(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W22703 / Serotype O:9 / Biotype 2; PLASMID=pYVe227;
RA Iriarte M., Lambermont I., Kerbourch C., Cornelis G.R.;
RT "Detailed genetic map of the pYVe227 plasmid of Yersinia enterocolitica
RT serotype O:9.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A127/90 / Serotype O:8 / Biotype 1B; PLASMID=pYVa127/90;
RX PubMed=14527656; DOI=10.1016/s0923-2508(03)00147-5;
RA Foultier B., Cornelis G.R.;
RT "DNA sequence and analysis of the pYVa127/90 virulence plasmid of Yersinia
RT enterocolitica strain A127/90.";
RL Res. Microbiol. 154:553-557(2003).
CC -!- FUNCTION: Functions as a specific chaperone for YopT.
CC {ECO:0000269|PubMed:9723929}.
CC -!- SUBUNIT: Binds to YopT. {ECO:0000269|PubMed:9723929}.
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DR EMBL; AF102990; AAD16809.1; -; Genomic_DNA.
DR EMBL; AY150843; AAN37556.1; -; Genomic_DNA.
DR RefSeq; NP_052386.1; NC_002120.1.
DR RefSeq; NP_783658.1; NC_004564.1.
DR RefSeq; NP_863508.1; NC_005017.1.
DR RefSeq; WP_005176720.1; NZ_NWMR01000110.1.
DR RefSeq; WP_010891204.1; NZ_SJZK01000009.1.
DR PDB; 2BHO; X-ray; 2.61 A; A=1-130.
DR PDB; 2BSH; X-ray; 1.90 A; A/B=2-122.
DR PDB; 2BSI; X-ray; 2.01 A; A/B=2-122.
DR PDB; 2BSJ; X-ray; 1.83 A; A/B=2-130.
DR PDBsum; 2BHO; -.
DR PDBsum; 2BSH; -.
DR PDBsum; 2BSI; -.
DR PDBsum; 2BSJ; -.
DR AlphaFoldDB; P0C2V9; -.
DR SMR; P0C2V9; -.
DR OMA; LEAWTEC; -.
DR OrthoDB; 2068985at2; -.
DR EvolutionaryTrace; P0C2V9; -.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR InterPro; IPR010261; Tir_chaperone.
DR Pfam; PF05932; CesT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Plasmid.
FT CHAIN 1..130
FT /note="Chaperone protein SycT"
FT /id="PRO_0000072369"
FT VARIANT 81
FT /note="S -> P (in plasmid pYVa127/90)"
FT VARIANT 114
FT /note="P -> S (in plasmid pYVa127/90)"
FT HELIX 5..16
FT /evidence="ECO:0007829|PDB:2BSJ"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2BSJ"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2BSJ"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2BSJ"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:2BSJ"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2BSJ"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:2BSJ"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:2BSJ"
FT HELIX 94..111
FT /evidence="ECO:0007829|PDB:2BSJ"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2BSJ"
SQ SEQUENCE 130 AA; 15158 MW; 2F0343C0836F52DF CRC64;
MQTTFTELMQ QLFLKLGLNH QVNENDVYTF EVDGHIQVLI ACYHQQWVQL FSELGADLPT
NDNLFGEHWP AHVQGRLDGK SILWSQQSLV GLDIDEMQAW LERFIDDIEQ RKEPQNTKFQ
PNSTSPILFI
