ID   SOPA_SALSV              Reviewed;         782 AA.
AC   B4TMK5;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=SeSA_A2237;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001127; ACF92447.1; -; Genomic_DNA.
DR   RefSeq; WP_000704007.1; NC_011094.1.
DR   AlphaFoldDB; B4TMK5; -.
DR   SMR; B4TMK5; -.
DR   EnsemblBacteria; ACF92447; ACF92447; SeSA_A2237.
DR   KEGG; sew:SeSA_A2237; -.
DR   HOGENOM; CLU_026158_0_0_6; -.
DR   OMA; ISEWIRP; -.
DR   Proteomes; UP000001865; 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_0000395855"
FT   REGION          133..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;  87274 MW;  131B7A6BEF23BC8D CRC64;
     MKISSGTINF STIPNQVKKL ITSIREHTKN GLASKITSVK NTHTSLNEKF KTGKDSPIEF
     TLPQKIKDFF QPKDKNTLNK TLITVKNIKD TNNTGKKNIS EEDASKMTAA FMRKHIANQS
     RDYNYRVTGA APLPGGVSVS ANNRPTVSEG RTPPVSPSLS LQATSSPSSP ADWAKKLTDA
     VLRQQAGEPL TTADRDFSNA DFRNIKFSKI LPPNFMKRDG DIIKGFNFSN SKFTYSDISH
     LHFDECRFTY STLNDVVCSN TKFSNSDMNE VSLLYSITTQ QQPSFINTTL KNTLIPHKAN
     LSDVILNEPD NSSPPSVSGG GNFIRLGDIW LQMPLLWTEN AVDGFLNHEH NNGKSILMTI
     NNLPDKYRQE KVRAMEDLVK SFRSGRLTEA RIRPVESSLV SVLAHPPYTQ SALISEWIRP
     VQERFFAHQC QTYNDVPLPA PDTYYQQRIL PVLLDSFDRN SAAMTTHSGL FNQVILHCMT
     GVDCTDGIRQ KAAALYEQYL AHPAVSPHIH NGLFGNYDGS PDWTTRAADN FLLLSSQDSD
     TAMMLSTDTL LTMLNPTPDT AWDNFYLLRA GENVSTAQIS PVELFRHDFP VFLAAFNQQA
     VQRRFGELID IILSTEEHGE LNQQFIAATN QKHSTVKLID DASVSRLNTI FDPLLPEGKL
     SPAHYQHILS AYHLTDATPQ KQAETLFCLS TAFARYSSSA IFGTEHDSPP ALRGYAEALM
     QKAWELSPAI FPSSEQFTDW SDRFHGLHGA FTCTSVVADS MQRHARKYFP SVLSSILPLA
     WA