ID   SOPA_SALDU              Reviewed;         782 AA.
AC   Q9S4P4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 45.
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;
OS   Salmonella dublin.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=98360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 55-64 AND 416-424,
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=2229;
RX   PubMed=11207586; DOI=10.1046/j.1462-5822.2000.00054.x;
RA   Wood M.W., Jones M.A., Watson P.R., Siber A.M., McCormick B.A., Hedges S.,
RA   Rosqvist R., Wallis T.S., Galyov E.E.;
RT   "The secreted effector protein of Salmonella dublin, SopA, is translocated
RT   into eukaryotic cells and influences the induction of enteritis.";
RL   Cell. Microbiol. 2:293-303(2000).
RN   [2]
RP   SUBCELLULAR LOCATION, AND DOMAIN.
RC   STRAIN=2229;
RX   PubMed=15866946; DOI=10.1128/jb.187.10.3565-3571.2005;
RA   Layton A.N., Brown P.J., Galyov E.E.;
RT   "The Salmonella translocated effector SopA is targeted to the mitochondria
RT   of infected cells.";
RL   J. Bacteriol. 187:3565-3571(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 (By
CC       similarity). Required for inducing polymorphonuclear leukocytes
CC       migration across the intestinal epithelium.
CC       {ECO:0000250|UniProtKB:Q8ZNR3, ECO:0000269|PubMed:11207586}.
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:0000269|PubMed:11207586}. Host
CC       mitochondrion {ECO:0000269|PubMed:15866946}. Note=Secreted via type III
CC       secretion system 1 (SPI-1 TTSS), and delivered into the host cell via a
CC       Sip-dependent pathway. Localizes to the mitochondria of host cell.
CC       {ECO:0000269|PubMed:15866946}.
CC   -!- DOMAIN: Amino acids 100 to 347 are sufficient to target SopA to the
CC       mitochondria. {ECO:0000269|PubMed:15866946}.
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   -!- DISRUPTION PHENOTYPE: Mutants are significantly less enteropathogenic
CC       that the wild-type strain in intestinal ligated loops and are impaired
CC       in their ability to promote polymorphonuclear leukocytes movements
CC       across the model epithelial monolayer. {ECO:0000269|PubMed:11207586}.
CC   -!- SIMILARITY: Belongs to the SopA E3 ligase family. {ECO:0000305}.
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DR   EMBL; AF121227; AAD46479.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S4P4; -.
DR   SMR; Q9S4P4; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0033650; C:host cell mitochondrion; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Host mitochondrion; Secreted; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway; Virulence.
FT   CHAIN           1..782
FT                   /note="E3 ubiquitin-protein ligase SopA"
FT                   /id="PRO_0000395848"
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"
FT   CONFLICT        417
FT                   /note="W -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   782 AA;  86885 MW;  B34FD41C8B57BF84 CRC64;
     MKISSGAINF STIPNQVKKL ITSIREHTKN GLASKITSVK NTHTSLNEKF KTGKDSPIEF
     ALPQKIKDFF QPKDKNTLNK TLITVKNIKD TNNAGKKNIS AEDVSKMNAA FMRKHIANQT
     CDYNYRMTGA APLPGGVSVS ANNRPTVSEG RTPPVSPSLS LQATSSPSSP ADWAKKLTDA
     VLRQKAGETL TAADRDFSNA DFRNITFSKI LPPSFMERDG DIIKGFNFSN SKFTYSDISH
     LHFDECRFTY STLSDVVCSN TKFSNSDMNE VVLQYSITTQ QQPSFIHTTL KNTLIRHKAN
     LSGVILNEPH NSSPPSVSGG GNFIRLGDIW LQMPLLWTEN AVDGFLNHEH NNGKSILMTI
     DSLPDKYSQE KVQAMEDLVK SLRGGRLTEA CIRPVESSLV SVLAHPPYTQ SALIREWLGP
     VQERFFAHQC QTYNDVPLPT PDTYYQQRIL PVLLDSFDRN SAAMTTHSGL FNQVILHCMT
     GVDCTDGTRQ KAAALYEQYL AHPAVSPHIH NGLFGNYDGS SDWTTRAADN FLLLSSQDSD
     TAMMLSTDTL LTMLNPTPDT AWDNFYLQRA GENVSTAQIS PVELFRHDFP VFLAAFNQQA
     TQRRFGELID IILSTEEHGE LNQQFLAATN QKHSTVKLID DASVSRLATI FDPLLPEGKL
     SPAHYQHILS AYHLTDATPQ KQAETLFCLS TAFARYSSSA IFGTEHDSPP ALRGYAEALM
     QKAWELSPAI FPTSEQFTDW SDRFHGLHGA FTCTCVVADS MQRHARKYFP SVLSSILPLS
     WA