ID   SOPA_SALCH              Reviewed;         782 AA.
AC   Q57MS9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   25-MAY-2022, entry version 64.
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=SCH_2076;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAX65982.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE017220; AAX65982.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q57MS9; -.
DR   SMR; Q57MS9; -.
DR   EnsemblBacteria; AAX65982; AAX65982; SCH_2076.
DR   KEGG; sec:SCH_2076; -.
DR   HOGENOM; CLU_026158_0_0_6; -.
DR   Proteomes; UP000000538; 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_0000395850"
FT   ACT_SITE        753
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   782 AA;  86968 MW;  D834B8C2A7206EAF CRC64;
     MKISSGAINF STIPNQVKKL ITSIREHTKN GFASKITSVK NTHASLNEKI KTGKSSSIEF
     ALPQKIKDFF QPKDKNTLNK TLITVKNIKD TNNAGKINIS AEDVSKMNAA FMRKHIANQS
     RDYNYRVTGA APLPGGVSVS ANNRPTVSEG RTPPVSPSLS LQATSFPSSP ADWAKKLTDA
     VLRQKAGETL TAADRDFSNA DFRNITFSKI LPPSFMERDG DIIKGFNFSN SKFTYSDISH
     LHFDECRFTY STLSDVVCSN TKFSNSDMNE VFLQYSITTQ QQPSFIDTTL KNTLIRHKAN
     LSGVILHEPD NSSPPSVSRG GNFIRLGDIW LQMPLLWTEN AVDGFLNHEH NNGKSILMTI
     DSLPDKYSQE KVRAMEDLVK SLRGGRLTEA GIRPVESSLV SVLAHPPYTQ SALISEWIRP
     VQERFFAHQC QTYNDVPLPA PDTYYQQRIL PVLLDSFDRN SAAMTTHSGL FNQVILHCMT
     GVDCTDGTRQ KAAALYEQYL AHPAVSPHIH NGLFGNYDGS PDWTTRAADN FLLLSSQDSD
     TAMMLSTNTL LTMLNPTPDT AWDNFYLLRA GENVSTAQIS PVELFRHDFP VFLAAFNQQA
     TQRRFGELID IILSTEEHGE LNQQFIAATN QKHSTVKLID DASVSRLNTI FDPLLPEGKL
     SPAHYQHILS AYHLTDATPQ KQAETLFCLS TAFARYSSSA IFGTEHDSPP ALRGYAEALM
     QKAWELSPAI FPSSEQFTDW SDRFHGLHGA FTCTSVVADS MQRHARKYFP SVLSSILPLA
     WA