ID   SOPA_SALA4              Reviewed;         782 AA.
AC   B5EX33;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-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=SeAg_B2190;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
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}.
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DR   EMBL; CP001138; ACH48508.1; -; Genomic_DNA.
DR   RefSeq; WP_000703987.1; NC_011149.1.
DR   AlphaFoldDB; B5EX33; -.
DR   SMR; B5EX33; -.
DR   EnsemblBacteria; ACH48508; ACH48508; SeAg_B2190.
DR   KEGG; sea:SeAg_B2190; -.
DR   HOGENOM; CLU_026158_0_0_6; -.
DR   OMA; ISEWIRP; -.
DR   Proteomes; UP000008819; 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_0000395849"
FT   REGION          140..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        753
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   782 AA;  86727 MW;  8B66ADA5F0273613 CRC64;
     MKISSGAINF STIPNQVKKL ITSIREHTKN GFASKITSVK NTHASLNEKL KTGKSSSIEF
     ALPQKIKDFF QPKDKNTLNK TLITVKNIKD TNNAGKKNIS AEDVSKMNAA FMRKHIANQT
     CDYNYRVTGA APLPGGVSVS ANNRPTVSEG RTPPVSPSLS LQATSSPSSP AEWAKKLTDA
     LLRQKAGETL TAADRDFSNA DFRNITFSKI LPTSFMKRDG DIIKGFNFSN SKFTYSDISH
     LHFDECRFTY STLSDVVCSN TKFSNSDMNE LTLQYSITTR QQPSFINTTL KNTFIRHKAN
     LSGVILNEPD NSSPPSVSGG GNFIRLGDIW LQMPLLWSEN AVDGFLNHEH NNGKSILMTI
     DSLPDKYSQE KVRAMEDLVK SLRGGRLTEA CIRPVESSLV SVLAHPPYTQ SALISEWLGP
     VQERFFAHQC QTYNDVPLPA PDTYYQQRIL PVLLDSFDRN SAAMTTHSGL FNQVILHCMT
     GVDCTDGTRQ KAAALYEQYL AHPAVSPHIH NGLFGNYDGS PDWTTRAADN FLLLSSQDSD
     TAMMLSTDTL LTMLNPTPDT AWDNFYLLRA GENVSTAQIS PVELFRHDFP VFLAAFNQQA
     TQRRFGELID IILSTEEHGE LNQQFIAATN QKHSTVKLID DASVSRLATI FDPLLPEGKL
     SPAHYQHILS AYHLTDATPQ KQAETLFCLS TAFARYSSSA IFGTEHDSPP ALRGYAEALM
     QKAWELSPAI FPSSEQFTEW SDRFHGLHGA FTCTSVVADS MQRHARKYFP SVLSSILPLA
     WA