SYCN_YERPE
ID SYCN_YERPE Reviewed; 123 AA.
AC P61380; P16162;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Chaperone protein SycN;
GN Name=sycN; OrderedLocusNames=YPCD1.37c, y5041, y0044, YP_pCD46;
OS Yersinia pestis.
OG Plasmid pCD1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=9746557; DOI=10.1128/iai.66.10.4611-4623.1998;
RA Perry R.D., Straley S.C., Fetherston J.D., Rose D.J., Gregor J.,
RA Blattner F.R.;
RT "DNA sequencing and analysis of the low-Ca2+-response plasmid pCD1 of
RT Yersinia pestis KIM5.";
RL Infect. Immun. 66:4611-4623(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=9748454; DOI=10.1128/jb.180.19.5192-5202.1998;
RA Hu P., Elliott J., McCready P., Skowronski E., Garnes J., Kobayashi A.,
RA Brubaker R.R., Garcia E.;
RT "Structural organization of virulence-associated plasmids of Yersinia
RT pestis.";
RL J. Bacteriol. 180:5192-5202(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=KIM5 / Biovar Mediaevalis, and KIM8;
RX PubMed=10094626; DOI=10.1046/j.1365-2958.1998.01110.x;
RA Day J.B., Plano G.V.;
RT "A complex composed of SycN and YscB functions as a specific chaperone for
RT YopN in Yersinia pestis.";
RL Mol. Microbiol. 30:777-788(1998).
RN [6]
RP FUNCTION.
RC STRAIN=KIM5 / Biovar Mediaevalis, and KIM8;
RX PubMed=12535078; DOI=10.1046/j.1365-2958.2003.03343.x;
RA Day J.B., Ferracci F., Plano G.V.;
RT "Translocation of YopE and YopN into eukaryotic cells by Yersinia pestis
RT yopN, tyeA, sycN, yscB and lcrG deletion mutants measured using a
RT phosphorylatable peptide tag and phosphospecific antibodies.";
RL Mol. Microbiol. 47:807-823(2003).
CC -!- FUNCTION: Functions as a specific chaperone for YopN. It could
CC facilitate the secretion and the subsequent translocation of YopN.
CC {ECO:0000269|PubMed:10094626, ECO:0000269|PubMed:12535078}.
CC -!- SUBUNIT: Interacts with YscB to form a complex which specifically binds
CC to YopN. {ECO:0000269|PubMed:10094626}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10094626}. Cell
CC inner membrane {ECO:0000269|PubMed:10094626}; Peripheral membrane
CC protein {ECO:0000269|PubMed:10094626}. Note=Not exported across the
CC inner membrane.
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DR EMBL; AF074612; AAC69794.1; -; Genomic_DNA.
DR EMBL; AF053946; AAC62567.1; -; Genomic_DNA.
DR EMBL; AL117189; CAB54914.1; -; Genomic_DNA.
DR EMBL; AE017043; AAS58565.1; -; Genomic_DNA.
DR PIR; T43588; T43588.
DR RefSeq; NP_395171.1; NC_003131.1.
DR RefSeq; NP_857745.1; NC_004836.1.
DR RefSeq; NP_857940.1; NC_004839.1.
DR RefSeq; WP_002229794.1; NZ_WHLN01000049.1.
DR PDB; 1XKP; X-ray; 1.70 A; B=1-123.
DR PDBsum; 1XKP; -.
DR AlphaFoldDB; P61380; -.
DR SMR; P61380; -.
DR STRING; 214092.5832457; -.
DR EnsemblBacteria; AAS58565; AAS58565; YP_pCD46.
DR GeneID; 66841111; -.
DR KEGG; ype:YPCD1.37c; -.
DR KEGG; ypm:YP_pCD46; -.
DR PATRIC; fig|214092.21.peg.48; -.
DR eggNOG; ENOG5033E8X; Bacteria.
DR HOGENOM; CLU_164012_0_0_6; -.
DR OMA; IQIDFEY; -.
DR EvolutionaryTrace; P61380; -.
DR Proteomes; UP000000815; Plasmid pCD1.
DR Proteomes; UP000001019; Plasmid pCD1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR InterPro; IPR012673; T3SS_SynN.
DR TIGRFAMs; TIGR02503; type_III_SycN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chaperone; Cytoplasm;
KW Membrane; Plasmid; Reference proteome.
FT CHAIN 1..123
FT /note="Chaperone protein SycN"
FT /id="PRO_0000072360"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:1XKP"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:1XKP"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1XKP"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 103..121
FT /evidence="ECO:0007829|PDB:1XKP"
SQ SEQUENCE 123 AA; 13609 MW; 3771F865B6E3D9AD CRC64;
MSWIEPIISH FCQDLGVPTS SPLSPLIQLE MAQSGTLQLE QHGATLTLWL ARSLAWHRCE
DAMVKALTLT AAQKSGALPL RAGWLGESQL VLFVSLDERS LTLPLLHQAF EQLLRLQQEV
LAP