ID   SOPA_SALTD              Reviewed;         782 AA.
AC   C9X8K0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
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=STMMW_20971;
OS   Salmonella typhimurium (strain D23580).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=568708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D23580;
RX   PubMed=19901036; DOI=10.1101/gr.091017.109;
RA   Kingsley R.A., Msefula C.L., Thomson N.R., Kariuki S., Holt K.E.,
RA   Gordon M.A., Harris D., Clarke L., Whitehead S., Sangal V., Marsh K.,
RA   Achtman M., Molyneux M.E., Cormican M., Parkhill J., Maclennan C.A.,
RA   Heyderman R.S., Dougan G.;
RT   "Epidemic multiple drug resistant Salmonella typhimurium causing invasive
RT   disease in sub-Saharan Africa have a distinct genotype.";
RL   Genome Res. 19:2279-2287(2009).
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       {ECO:0000250|UniProtKB:Q8ZNR3}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8ZNR3}. Host
CC       cell {ECO:0000250|UniProtKB:Q8ZNR3}. Note=Secreted via type III
CC       secretion system 1 (SPI-1 TTSS), and delivered into the host cell.
CC       {ECO:0000250|UniProtKB:Q8ZNR3}.
CC   -!- PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating
CC       enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin.
CC       {ECO:0000250|UniProtKB:Q8ZNR3}.
CC   -!- SIMILARITY: Belongs to the SopA E3 ligase family. {ECO:0000305}.
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DR   EMBL; FN424405; CBG25106.1; -; Genomic_DNA.
DR   RefSeq; WP_000703995.1; NC_016854.1.
DR   AlphaFoldDB; C9X8K0; -.
DR   SMR; C9X8K0; -.
DR   KEGG; sev:STMMW_20971; -.
DR   PATRIC; fig|568708.3.peg.2215; -.
DR   HOGENOM; CLU_026158_0_0_6; -.
DR   OMA; ISEWIRP; -.
DR   BioCyc; SENT568708:STMMW_RS10820-MON; -.
DR   Proteomes; UP000002622; 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; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS: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   3: Inferred from homology;
KW   Secreted; Transferase; Ubl conjugation; Ubl conjugation pathway; Virulence.
FT   CHAIN           1..782
FT                   /note="E3 ubiquitin-protein ligase SopA"
FT                   /id="PRO_0000395857"
FT   REGION          136..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:0000250"
SQ   SEQUENCE   782 AA;  86753 MW;  E7F7512B3A017E6A CRC64;
     MKISSGAINF STIPNQVKKL ITSIREHTKN GLTSKITSVK NTHTSLNEKF KTGKDSPIEF
     ALPQKIKDFF QPKDKNTLNK TLITVKNIKD TNNAGKKNIS AEDVSKMNAA FMRKHIANQT
     CDYNYRMTGA APLPGGVSVS ANNRPTVSEG RTPPVSPSLS LQATSSPSSP ADWAKKLTDA
     VLRQKAGEAL 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