SPAK_SALTY
ID SPAK_SALTY Reviewed; 135 AA.
AC P0A1N0; P39443;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Surface presentation of antigens protein SpaK;
DE AltName: Full=Class 1B type III secretion system chaperone SpaK;
DE AltName: Full=Invasion protein InvB;
GN Name=spaK; Synonyms=invB; OrderedLocusNames=STM2895;
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 [GENOMIC DNA].
RC STRAIN=SR-11;
RX PubMed=8045880; DOI=10.1128/jb.176.15.4501-4510.1994;
RA Eichelberg K., Ginocchio C.C., Galan J.E.;
RT "Molecular and functional characterization of the Salmonella typhimurium
RT invasion genes invB and invC: homology of InvC to the F0F1 ATPase family of
RT proteins.";
RL J. Bacteriol. 176:4501-4510(1994).
RN [2]
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 [3]
RP FUNCTION, AND INTERACTION WITH SOPA.
RC STRAIN=SL1344;
RX PubMed=16547027; DOI=10.1128/jb.188.7.2411-2420.2006;
RA Higashide W., Zhou D.;
RT "The first 45 amino acids of SopA are necessary for InvB binding and SPI-1
RT secretion.";
RL J. Bacteriol. 188:2411-2420(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SIPA, SUBUNIT, AND
RP FUNCTION.
RX PubMed=16507363; DOI=10.1016/j.molcel.2006.01.026;
RA Lilic M., Vujanac M., Stebbins C.E.;
RT "A common structural motif in the binding of virulence factors to bacterial
RT secretion chaperones.";
RL Mol. Cell 21:653-664(2006).
CC -!- FUNCTION: Involved in a secretory pathway responsible for the surface
CC presentation of determinants needed for the entry of Salmonella species
CC into mammalian cells. Chaperone specialized in the storage of effectors
CC within the bacterial cytoplasm, maintaining them in a secretion-
CC competent state, and allowing their immediate delivery to target cells
CC upon contact of the bacterium with the host cells. Has been shown to
CC chaperone SopA, SopE, SopE2 and SipA. {ECO:0000269|PubMed:16507363,
CC ECO:0000269|PubMed:16547027}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16507363}.
CC -!- SIMILARITY: Belongs to the SpaK family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U08279; AAA74037.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21775.1; -; Genomic_DNA.
DR RefSeq; NP_461816.1; NC_003197.2.
DR RefSeq; WP_001164066.1; NC_003197.2.
DR PDB; 2FM8; X-ray; 2.20 A; A/B=1-134.
DR PDBsum; 2FM8; -.
DR AlphaFoldDB; P0A1N0; -.
DR SMR; P0A1N0; -.
DR STRING; 99287.STM2895; -.
DR PaxDb; P0A1N0; -.
DR EnsemblBacteria; AAL21775; AAL21775; STM2895.
DR GeneID; 1254418; -.
DR KEGG; stm:STM2895; -.
DR PATRIC; fig|99287.12.peg.3051; -.
DR HOGENOM; CLU_125441_1_0_6; -.
DR OMA; TIMEGCQ; -.
DR BioCyc; SENT99287:STM2895-MON; -.
DR EvolutionaryTrace; P0A1N0; -.
DR PHI-base; PHI:646; -.
DR Proteomes; UP000001014; Chromosome.
DR InterPro; IPR003065; Invas_SpaK.
DR Pfam; PF03519; Invas_SpaK; 1.
DR PRINTS; PR01305; SSPAKPROTEIN.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Reference proteome; Virulence.
FT CHAIN 1..135
FT /note="Surface presentation of antigens protein SpaK"
FT /id="PRO_0000180965"
FT CONFLICT 87
FT /note="Missing (in Ref. 1; AAA74037)"
FT /evidence="ECO:0000305"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:2FM8"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2FM8"
FT STRAND 29..40
FT /evidence="ECO:0007829|PDB:2FM8"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2FM8"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:2FM8"
FT HELIX 62..78
FT /evidence="ECO:0007829|PDB:2FM8"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2FM8"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2FM8"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:2FM8"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2FM8"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2FM8"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:2FM8"
SQ SEQUENCE 135 AA; 14919 MW; 5F2A1EE477F9D684 CRC64;
MQHLDIAELV RSALEVSGCD PSLIGGIDSH STIVLDLFAL PSICISVKDD DVWIWAQLGA
DSMVVLQQRA YEILMTIMEG CHFARGGQLL LGEQNGELTL KALVHPDFLS DGEKFSTALN
GFYNYLEVFS RSLMR
