SOPD_SALTY
ID SOPD_SALTY Reviewed; 317 AA.
AC P40722;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Secreted effector protein SopD;
DE AltName: Full=Salmonella outer protein D;
GN Name=sopD; OrderedLocusNames=STM2945;
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=LT2;
RX PubMed=2670946; DOI=10.1016/s0021-9258(19)84893-7;
RA Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M.,
RA Kredich N.M.;
RT "Characterization of the cysJIH regions of Salmonella typhimurium and
RT Escherichia coli B. DNA sequences of cysI and cysH and a model for the
RT siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on
RT amino acid homology with spinach nitrite reductase.";
RL J. Biol. Chem. 264:15726-15737(1989).
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 SUBCELLULAR LOCATION.
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 [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-37 AND PHE-44.
RC STRAIN=SL1344;
RX PubMed=17696999; DOI=10.1111/j.1462-5822.2007.01000.x;
RA Bakowski M.A., Cirulis J.T., Brown N.F., Finlay B.B., Brumell J.H.;
RT "SopD acts cooperatively with SopB during Salmonella enterica serovar
RT Typhimurium invasion.";
RL Cell. Microbiol. 9:2839-2855(2007).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. Contributes to replication
CC in macrophages. Plays a role, cooperatively with SopB, in membrane
CC fission and macropinosome formation during invasion.
CC {ECO:0000269|PubMed:15554961, ECO:0000269|PubMed:17696999}.
CC -!- SUBCELLULAR LOCATION: Secreted. Host cytoplasm. Host cell membrane.
CC Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2
CC TTSS), and delivered into the host cell (Probable). Membrane-associated
CC in transfected cells. Recruited to the bacterial invasion site, and
CC this recruitment requires the phosphatase activity of SopB.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene impairs bacterial
CC replication in mouse macrophages but not in human epithelial cells.
CC {ECO:0000269|PubMed:15554961}.
CC -!- SIMILARITY: Belongs to the SopD family. {ECO:0000305}.
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DR EMBL; M23007; AAA27049.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21825.1; -; Genomic_DNA.
DR RefSeq; NP_461866.1; NC_003197.2.
DR RefSeq; WP_001145543.1; NC_003197.2.
DR PDB; 5CPC; X-ray; 2.15 A; A/B=1-317.
DR PDB; 7BWT; X-ray; 2.30 A; A=2-317.
DR PDBsum; 5CPC; -.
DR PDBsum; 7BWT; -.
DR AlphaFoldDB; P40722; -.
DR SMR; P40722; -.
DR STRING; 99287.STM2945; -.
DR PaxDb; P40722; -.
DR EnsemblBacteria; AAL21825; AAL21825; STM2945.
DR GeneID; 1254468; -.
DR KEGG; stm:STM2945; -.
DR PATRIC; fig|99287.12.peg.3106; -.
DR HOGENOM; CLU_072577_0_0_6; -.
DR OMA; CCINNVV; -.
DR PhylomeDB; P40722; -.
DR BioCyc; SENT99287:STM2945-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044164; C:host cell cytosol; IDA:UniProtKB.
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; IMP:AgBase.
DR InterPro; IPR022747; SopD.
DR Pfam; PF11047; SopD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cell membrane; Host cytoplasm; Host membrane; Membrane;
KW Reference proteome; Secreted; Virulence.
FT CHAIN 1..317
FT /note="Secreted effector protein SopD"
FT /id="PRO_0000072040"
FT MUTAGEN 37
FT /note="W->A: Localizes almost exclusively to the cytosol of
FT transfected cells."
FT /evidence="ECO:0000269|PubMed:17696999"
FT MUTAGEN 44
FT /note="F->A: Localizes almost exclusively to the cytosol of
FT transfected cells."
FT /evidence="ECO:0000269|PubMed:17696999"
FT CONFLICT 214
FT /note="M -> V (in Ref. 1; AAA27049)"
FT /evidence="ECO:0000305"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:5CPC"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5CPC"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:5CPC"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:5CPC"
FT TURN 225..231
FT /evidence="ECO:0007829|PDB:5CPC"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:5CPC"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:7BWT"
FT HELIX 264..283
FT /evidence="ECO:0007829|PDB:5CPC"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:5CPC"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5CPC"
SQ SEQUENCE 317 AA; 36141 MW; 2EF94AF11A9DE0F2 CRC64;
MPVTLSFGNH QNYTLNESRL AHLLSADKEK AIHMGGWDKV QDHFRAEKKD HALEVLHSII
HGQGRGEPGE MEVNVEDINK IYAFKRLQHL ACPAHQDLFT IKMDASQTQF LLMVGDTVIS
QSNIKDILNI SDDAVIESMS REERQLFLQI CEVIGSKMTW HPELLQESIS TLRKEVTGNA
QIKTAVYEMM RPAEAPDHPL VEWQDSLTAD EKSMLACINA GNFEPTTQFC KIGYQEVQGE
VAFSMMHPCI SYLLHSYSPF SEFKPTNSGF LKKLNQDYND YHAKKMFIDV ILEKLYLTHE
RSLHIGKDGC SRNILLT
