SOPD2_SALTY
ID SOPD2_SALTY Reviewed; 319 AA.
AC Q8ZQC8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Secreted effector protein sopD2;
DE AltName: Full=Salmonella outer protein D 2;
GN Name=sopD2; OrderedLocusNames=STM0972;
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 SUBCELLULAR LOCATION, SECRETION VIA TYPE III SECRETION SYSTEM, INDUCTION,
RP DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=SL1344;
RX PubMed=12535274; DOI=10.1034/j.1600-0854.2003.40106.x;
RA Brumell J.H., Kujat-Choy S., Brown N.F., Vallance B.A., Knodler L.A.,
RA Finlay B.B.;
RT "SopD2 is a novel type III secreted effector of Salmonella typhimurium that
RT targets late endocytic compartments upon delivery into host cells.";
RL Traffic 4:36-48(2003).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=SL1344;
RX PubMed=15554961; DOI=10.1111/j.1365-2958.2004.04344.x;
RA Jiang X., Rossanese O.W., Brown N.F., Kujat-Choy S., Galan J.E.,
RA Finlay B.B., Brumell J.H.;
RT "The related effector proteins SopD and SopD2 from Salmonella enterica
RT serovar Typhimurium contribute to virulence during systemic infection of
RT mice.";
RL Mol. Microbiol. 54:1186-1198(2004).
RN [4]
RP DOMAIN, AND MUTAGENESIS OF TRP-37 AND PHE-44.
RC STRAIN=SL1344;
RX PubMed=16849798; DOI=10.1099/mic.0.28995-0;
RA Brown N.F., Szeto J., Jiang X., Coombes B.K., Finlay B.B., Brumell J.H.;
RT "Mutational analysis of Salmonella translocated effector members SifA and
RT SopD2 reveals domains implicated in translocation, subcellular localization
RT and function.";
RL Microbiology 152:2323-2343(2006).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. Contributes to the
CC formation of Salmonella-induced filaments (Sifs) in infected epithelial
CC cells and to replication in macrophages. {ECO:0000269|PubMed:15554961}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12535274}. Host cell
CC membrane {ECO:0000269|PubMed:12535274}. Note=Secreted via type III
CC secretion system 2 (SPI-2 TTSS), and delivered into the host cell.
CC Membrane-associated. Localizes to the Salmonella-containing vacuole
CC (SCV) in infected cells and to late endocytic compartments in
CC transfected cells.
CC -!- INDUCTION: Transcription is induced inside host cells and is dependent
CC on the SsrA/SsrB and PhoP/PhoQ two-component systems.
CC {ECO:0000269|PubMed:12535274}.
CC -!- DOMAIN: The N-terminal domain mediates secretion by SPI-2 TTSS and
CC targeting of late endocytic compartments in host cells.
CC {ECO:0000269|PubMed:12535274, ECO:0000269|PubMed:16849798}.
CC -!- DISRUPTION PHENOTYPE: Mutation leads to a prolonged survival of
CC infected mice. Deletion blocks Sifs formation at an intermediate stage,
CC before fusion of late endosome compartments with the SCV, and impairs
CC bacterial replication in mouse macrophages but not in human epithelial
CC cells. {ECO:0000269|PubMed:12535274, ECO:0000269|PubMed:15554961}.
CC -!- SIMILARITY: Belongs to the SopD family. {ECO:0000305}.
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DR EMBL; AE006468; AAL19906.1; -; Genomic_DNA.
DR RefSeq; NP_459947.1; NC_003197.2.
DR RefSeq; WP_001145561.1; NC_003197.2.
DR PDB; 5CQ9; X-ray; 3.00 A; A/B=1-319.
DR PDBsum; 5CQ9; -.
DR AlphaFoldDB; Q8ZQC8; -.
DR SMR; Q8ZQC8; -.
DR STRING; 99287.STM0972; -.
DR PaxDb; Q8ZQC8; -.
DR EnsemblBacteria; AAL19906; AAL19906; STM0972.
DR GeneID; 1252490; -.
DR KEGG; stm:STM0972; -.
DR PATRIC; fig|99287.12.peg.1025; -.
DR HOGENOM; CLU_072577_0_0_6; -.
DR OMA; ELFFKVC; -.
DR PhylomeDB; Q8ZQC8; -.
DR BioCyc; SENT99287:STM0972-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IDA:UniProtKB.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IDA:UniProtKB.
DR DisProt; DP02655; -.
DR InterPro; IPR022747; SopD.
DR Pfam; PF11047; SopD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cell membrane; Host membrane; Membrane;
KW Reference proteome; Secreted; Virulence.
FT CHAIN 1..319
FT /note="Secreted effector protein sopD2"
FT /id="PRO_0000392204"
FT MOTIF 37..44
FT /note="Required to target late endocytic compartments"
FT MUTAGEN 37
FT /note="W->P: Localizes throughout the cytosol and not to
FT late endocytic compartments; when associated with R-44."
FT /evidence="ECO:0000269|PubMed:16849798"
FT MUTAGEN 44
FT /note="F->R: Localizes throughout the cytosol and not to
FT late endocytic compartments; when associated with P-37."
FT /evidence="ECO:0000269|PubMed:16849798"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5CQ9"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5CQ9"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:5CQ9"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:5CQ9"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:5CQ9"
FT TURN 225..231
FT /evidence="ECO:0007829|PDB:5CQ9"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:5CQ9"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:5CQ9"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:5CQ9"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5CQ9"
SQ SEQUENCE 319 AA; 37782 MW; 59060CEC9FA0F4F5 CRC64;
MPVTLSFGNR HNYEINHSRL ARLMSPDKEE ALYMGVWDRF KDCFRTHKKQ EVLEVLYTLI
HGCERENQAE LNVDITGMEK IHAFTQLKEY ANPSQQDRFV MRFDMNQTQV LFEIDGKVID
KCNLHRLLNV SENCIFKVME EDEEELFLKI CIKYGEKISR YPELLEGFAN KLKDAVNEDD
DVKDEVYKLM RSGEDRKMEC VEWNGTLTEE EKNKLRCLQM GSFNITTQFF KIGYWELEGE
VLFDMVHPTL SYLLQAYKPS LSSDLIETNT MLFSDVLNKD YDDYQNNKRE IDAILRRIYR
SHNNTLFISE KSSCRNMLI
