ID   SOPA_SALEP              Reviewed;         782 AA.
AC   B5QZK6;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=SEN2065;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(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       {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; AM933172; CAR33644.1; -; Genomic_DNA.
DR   RefSeq; WP_000703991.1; NC_011294.1.
DR   AlphaFoldDB; B5QZK6; -.
DR   SMR; B5QZK6; -.
DR   KEGG; set:SEN2065; -.
DR   HOGENOM; CLU_026158_0_0_6; -.
DR   OMA; ISEWIRP; -.
DR   Proteomes; UP000000613; 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_0000395852"
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:0000250"
SQ   SEQUENCE   782 AA;  86692 MW;  4B77B738FEDBA613 CRC64;
     MKISSGAINF STIPNQVKKL ITSIREHTKN GLASKITSVK NTHASLNEKL KTGKSSSIEF
     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 SALIREWLGP
     VQERFFAHQC QTYNDVPLPT PDTYYQQRIL PVLLDSFDRN SAAMTTHSGL FNQVILHCMT
     GVDCTDGTRQ KAAALYEQYL AHPAVSPHIH NGLFGNYDGS PDWTTRAADN FLLLSSQDSD
     TAMMLSTDTL LTMLNPTPDT AWDNFYLLRA GENVSTAQIS PVELFRHDFP VFLAAFNQQA
     TQRRFGELID IILSTEEHGE LNQQFIAATN QKHSTVKLID DASVSRLATI FAPLLPEGKL
     SPAHYQHILS AYHLTDATPQ KQAETLFCLS TAFARYSSSA IFGTEHDSPP ALRGYAEALM
     QKAWELSPAI FPSSEQFTDW SDRFHGLHGA FTCTSVVADS MQRHARKYFP SVLSSILPLA
     WA