SOPA_SALTY
ID SOPA_SALTY Reviewed; 782 AA.
AC Q8ZNR3;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=E3 ubiquitin-protein ligase SopA;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase SopA {ECO:0000305};
DE AltName: Full=Salmonella outer protein A;
DE AltName: Full=Secreted effector protein SopA;
GN Name=sopA; OrderedLocusNames=STM2066;
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 INTERACTION WITH SPAK/INVB.
RC STRAIN=SL1344;
RX PubMed=14762020; DOI=10.1128/jb.186.4.1215-1219.2004;
RA Ehrbar K., Hapfelmeier S., Stecher B., Hardt W.D.;
RT "InvB is required for type III-dependent secretion of SopA in Salmonella
RT enterica serovar Typhimurium.";
RL J. Bacteriol. 186:1215-1219(2004).
RN [3]
RP INTERACTION WITH SPAK/INVB, SUBCELLULAR LOCATION, AND DOMAIN.
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 FUNCTION, UBIQUITIN LIGASE ACTIVITY, UBIQUITINATION, AND MUTAGENESIS OF
RP CYS-753.
RC STRAIN=SL1344;
RX PubMed=17076670; DOI=10.1111/j.1365-2958.2006.05407.x;
RA Zhang Y., Higashide W.M., McCormick B.A., Chen J., Zhou D.;
RT "The inflammation-associated Salmonella SopA is a HECT-like E3 ubiquitin
RT ligase.";
RL Mol. Microbiol. 62:786-793(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 163-782, FUNCTION AS A LIGASE,
RP DOMAIN, AND MUTAGENESIS OF LEU-747 AND THR-752.
RX PubMed=18066077; DOI=10.1038/nsmb1346;
RA Diao J., Zhang Y., Huibregtse J.M., Zhou D., Chen J.;
RT "Crystal structure of SopA, a Salmonella effector protein mimicking a
RT eukaryotic ubiquitin ligase.";
RL Nat. Struct. Mol. Biol. 15:65-70(2008).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. This protein is an E3
CC ubiquitin ligase that interferes with host's ubiquitination pathway.
CC Required for inducing polymorphonuclear leukocytes migration across the
CC intestinal epithelium. Preferentially uses host UBE2D1 (UBCH5A), UBE2D2
CC (UBCH5B) and UBE2L3 (UBCH7) as E2 ubiquitin-conjugating enzymes.
CC {ECO:0000269|PubMed:17076670, ECO:0000269|PubMed:18066077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26;
CC -!- SUBUNIT: Interacts with SpaK/InvB. {ECO:0000269|PubMed:14762020,
CC ECO:0000269|PubMed:16547027}.
CC -!- INTERACTION:
CC Q8ZNR3; P68036-1: UBE2L3; Xeno; NbExp=2; IntAct=EBI-15674008, EBI-15556257;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16547027}. Host cell
CC {ECO:0000269|PubMed:16547027}. Note=Secreted via type III secretion
CC system 1 (SPI-1 TTSS), and delivered into the host cell. Can also be
CC secreted through the flagellar export apparatus.
CC {ECO:0000269|PubMed:16547027}.
CC -!- DOMAIN: The N-terminal 45 amino acids are necessary and sufficient for
CC secretion and translocation into host cells. This N-terminal region
CC binds the SpaK/InvB chaperone. Contains a C-terminal HECT-like domain.
CC {ECO:0000269|PubMed:16547027, ECO:0000269|PubMed:18066077}.
CC -!- PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating
CC enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin.
CC {ECO:0000269|PubMed:17076670}.
CC -!- MISCELLANEOUS: Requires SpaK/InvB as a chaperone for its stability and
CC for secretion.
CC -!- SIMILARITY: Belongs to the SopA E3 ligase family. {ECO:0000305}.
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DR EMBL; AE006468; AAL20970.1; -; Genomic_DNA.
DR RefSeq; NP_461011.1; NC_003197.2.
DR RefSeq; WP_000703998.1; NC_003197.2.
DR PDB; 2QYU; X-ray; 2.10 A; A=163-782.
DR PDB; 2QZA; X-ray; 2.80 A; A/B=165-782.
DR PDB; 3SY2; X-ray; 3.27 A; A/B=165-782.
DR PDB; 5JW7; X-ray; 2.85 A; A=163-425.
DR PDBsum; 2QYU; -.
DR PDBsum; 2QZA; -.
DR PDBsum; 3SY2; -.
DR PDBsum; 5JW7; -.
DR AlphaFoldDB; Q8ZNR3; -.
DR SMR; Q8ZNR3; -.
DR DIP; DIP-46397N; -.
DR IntAct; Q8ZNR3; 1.
DR STRING; 90371.CY43_11145; -.
DR PaxDb; Q8ZNR3; -.
DR EnsemblBacteria; AAL20970; AAL20970; STM2066.
DR GeneID; 1253587; -.
DR KEGG; stm:STM2066; -.
DR PATRIC; fig|99287.12.peg.2188; -.
DR HOGENOM; CLU_026158_0_0_6; -.
DR OMA; ISEWIRP; -.
DR PhylomeDB; Q8ZNR3; -.
DR BioCyc; SENT99287:STM2066-MON; -.
DR EvolutionaryTrace; Q8ZNR3; -.
DR PHI-base; PHI:7919; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR Gene3D; 1.10.4140.10; -; 1.
DR InterPro; IPR025725; SopA-like_cat.
DR InterPro; IPR038270; SopA-like_catalytic_sf.
DR InterPro; IPR025726; SopA-like_central.
DR Pfam; PF13981; SopA; 1.
DR Pfam; PF13979; SopA_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Secreted; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Virulence.
FT CHAIN 1..782
FT /note="E3 ubiquitin-protein ligase SopA"
FT /id="PRO_0000395847"
FT REGION 137..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 753
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 747
FT /note="L->A: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:18066077"
FT MUTAGEN 752
FT /note="T->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:18066077"
FT MUTAGEN 753
FT /note="C->S: Loss of ubiquitin ligase activity. No
FT thioester formation."
FT /evidence="ECO:0000269|PubMed:17076670"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:2QYU"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2QZA"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:5JW7"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:2QYU"
FT TURN 349..353
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 412..433
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 450..459
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 468..480
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 486..501
FT /evidence="ECO:0007829|PDB:2QYU"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:2QYU"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 547..554
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 581..588
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 590..612
FT /evidence="ECO:0007829|PDB:2QYU"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 619..628
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 641..651
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 652..654
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 662..671
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:2QZA"
FT HELIX 679..696
FT /evidence="ECO:0007829|PDB:2QYU"
FT TURN 699..702
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 710..726
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 734..744
FT /evidence="ECO:0007829|PDB:2QYU"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:2QZA"
FT HELIX 756..768
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 770..776
FT /evidence="ECO:0007829|PDB:2QYU"
FT HELIX 779..781
FT /evidence="ECO:0007829|PDB:2QYU"
SQ SEQUENCE 782 AA; 86783 MW; 1D56B53EC05EDB94 CRC64;
MKISSGAINF STIPNQVKKL ITSIREHTKN GLTSKITSVK NTHTSLNEKF KTGKDSPIEF
ALPQKIKDFF QPKDKNTLNK TLITVKNIKD TNNAGKKNIS AEDVSKMNAA FMRKHIANQT
CDYNYRMTGA APLPGGVSVS ANNRPTVSEG RTPPVSPSLS LQATSSPSSP ADWAKKLTDA
VLRQKAGETL TAADRDFSNA DFRNITFSKI LPPSFMERDG DIIKGFNFSN SKFTYSDISH
LHFDECRFTY STLSDVVCSN TKFSNSDMNE VFLQYSITTQ QQPSFIDTTL KNTLIRHKAN
LSGVILNEPD NSSPPSVSGG GNFIRLGDIW LQMPLLWTEN AVDGFLNHEH NNGKSILMTI
DSLPDKYSQE KVQAMEDLVK SLRGGRLTEA CIRPVESSLV SVLAHPPYTQ SALISEWLGP
VQERFFAHQC QTYNDVPLPA PDTYYQQRIL PVLLDSFDRN SAAMTTHSGL FNQVILHCMT
GVDCTDGTRQ KAAALYEQYL AHPAVSPHIH NGLFGNYDGS PDWTTRAADN FLLLSSQDSD
TAMMLSTDTL LTMLNPTPDT AWDNFYLLRA GENVSTAQIS PVELFRHDFP VFLAAFNQQA
TQRRFGELID IILSTEEHGE LNQQFLAATN QKHSTVKLID DASVSRLATI FDPLLPEGKL
SPAHYQHILS AYHLTDATPQ KQAETLFCLS TAFARYSSSA IFGTEHDSPP ALRGYAEALM
QKAWELSPAI FPSSEQFTEW SDRFHGLHGA FTCTSVVADS MQRHARKYFP SVLSSILPLA
WA
