ID   SICP_SALTY              Reviewed;         116 AA.
AC   P0CL16; O85300; Q8ZMI1;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Chaperone protein SicP;
GN   Name=sicP; OrderedLocusNames=STM2879;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION.
RC   STRAIN=SL1344;
RX   PubMed=9642193; DOI=10.1128/jb.180.13.3393-3399.1998;
RA   Fu Y., Galan J.E.;
RT   "Identification of a specific chaperone for SptP, a substrate of the
RT   centisome 63 type III secretion system of Salmonella typhimurium.";
RL   J. Bacteriol. 180:3393-3399(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 4-116 IN COMPLEX WITH SPTP.
RX   PubMed=11689946; DOI=10.1038/35102073;
RA   Stebbins C.E., Galan J.E.;
RT   "Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial
RT   type III secretion.";
RL   Nature 414:77-81(2001).
CC   -!- FUNCTION: Molecular chaperone required for SptP stabilization and
CC       secretion. {ECO:0000269|PubMed:9642193}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: The structure of the SptP-SicP complex contains four
CC       molecules of the chaperone SicP, aligned in a linear fashion and
CC       arranged in two sets of tightly bound homodimers that bind two SptP
CC       molecules. The SicP homodimers do not interact with each other, but are
CC       held together by a molecular interface formed between two SptP
CC       molecules. The chaperone-binding domain of SptP does not adopt a
CC       globular fold for interaction with SicP. Each SptP molecule is wrapped
CC       around by three SicP chaperones (two chaperones from one homodimer and
CC       a third one from the opposite homodimer pair). SptP interacts with SicP
CC       chaperone dimers mainly through four regions of its chaperone-binding
CC       domain.
CC   -!- SIMILARITY: Belongs to the SicP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL21759.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE006468; AAL21759.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_461800.1; NC_003197.2.
DR   PDB; 1JYO; X-ray; 1.90 A; A/B/C/D=2-116.
DR   PDBsum; 1JYO; -.
DR   AlphaFoldDB; P0CL16; -.
DR   SMR; P0CL16; -.
DR   IntAct; P0CL16; 1.
DR   STRING; 99287.STM2879; -.
DR   PaxDb; P0CL16; -.
DR   EnsemblBacteria; AAL21759; AAL21759; STM2879.
DR   GeneID; 1254402; -.
DR   KEGG; stm:STM2879; -.
DR   PATRIC; fig|99287.12.peg.3035; -.
DR   HOGENOM; CLU_126979_0_0_6; -.
DR   OMA; TELANMY; -.
DR   EvolutionaryTrace; P0CL16; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR   CDD; cd17021; T3SC_IA_SicP-like; 1.
DR   InterPro; IPR044530; SicP.
DR   InterPro; IPR010261; Tir_chaperone.
DR   Pfam; PF05932; CesT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Reference proteome; Virulence.
FT   CHAIN           1..116
FT                   /note="Chaperone protein SicP"
FT                   /id="PRO_0000097754"
FT   STRAND          11..17
FT                   /evidence="ECO:0007829|PDB:1JYO"
FT   TURN            18..20
FT                   /evidence="ECO:0007829|PDB:1JYO"
FT   STRAND          21..28
FT                   /evidence="ECO:0007829|PDB:1JYO"
FT   STRAND          31..40
FT                   /evidence="ECO:0007829|PDB:1JYO"
FT   HELIX           47..62
FT                   /evidence="ECO:0007829|PDB:1JYO"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:1JYO"
FT   TURN            72..75
FT                   /evidence="ECO:0007829|PDB:1JYO"
FT   STRAND          76..83
FT                   /evidence="ECO:0007829|PDB:1JYO"
FT   HELIX           89..110
FT                   /evidence="ECO:0007829|PDB:1JYO"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:1JYO"
SQ   SEQUENCE   116 AA;  12936 MW;  20FA6FF5A0B6973F CRC64;
     MGLPLTFDDN NQCLLLLDSD IFTSIEAKDD IWLLNGMIIP LSPVCGDSIW RQIMVINGEL
     AANNEGTLAY IDAAETLLLI HAITDLTNTY HIISQLESFV NQQEALKNIL QEYAKV