ID   CDIA8_BURPE             Reviewed;        1269 AA.
AC   H9T8G4;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=tRNA nuclease CdiA;
DE            EC=3.1.-.-;
DE   AltName: Full=Toxin CdiA;
DE   Flags: Fragment;
GN   Name=cdiA;
OS   Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=28450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=E478;
RX   PubMed=18299706; DOI=10.1371/journal.pntd.0000182;
RA   Chantratita N., Wuthiekanun V., Limmathurotsakul D., Vesaratchavest M.,
RA   Thanwisai A., Amornchai P., Tumapa S., Feil E.J., Day N.P., Peacock S.J.;
RT   "Genetic diversity and microevolution of Burkholderia pseudomallei in the
RT   environment.";
RL   PLoS Negl. Trop. Dis. 2:E182-E182(2008).
RN   [2]
RP   FUNCTION, INTERACTION WITH CDII, SUBUNIT, DOMAIN, EXPRESSION IN E.COLI, AND
RP   MUTAGENESIS OF ASP-1263.
RC   STRAIN=E478;
RX   PubMed=22435733; DOI=10.1111/j.1365-2958.2012.08039.x;
RA   Nikolakakis K., Amber S., Wilbur J.S., Diner E.J., Aoki S.K., Poole S.J.,
RA   Tuanyok A., Keim P.S., Peacock S., Hayes C.S., Low D.A.;
RT   "The toxin/immunity network of Burkholderia pseudomallei contact-dependent
RT   growth inhibition (CDI) systems.";
RL   Mol. Microbiol. 84:516-529(2012).
CC   -!- FUNCTION: Toxic component of a toxin-immunity protein module, which
CC       functions as a cellular contact-dependent growth inhibition (CDI)
CC       system. CDI modules allow bacteria to communicate with and inhibit the
CC       growth of closely related neighboring bacteria in a contact-dependent
CC       fashion. The C-terminal 282 residues (CT domain) acts as a tRNA
CC       endonuclease on some (tRNA1(Tyr), tRNA(Asn), tRNA(His)), but not all
CC       E.coli tRNAs, and inhibits growth in E.coli. Toxic activity is
CC       neutralized by coexpression of the cognate immunity protein CdiI in
CC       E.coli, but not by non-cognate immunity proteins from other strains of
CC       B.pseudomallei. {ECO:0000269|PubMed:22435733}.
CC   -!- FUNCTION: The CdiA protein is thought to be exported from the cell
CC       through the central lumen of CdiB, the other half of its two-partner
CC       system (TPS). The TPS domain probably remains associated with CdiB
CC       while the FHA-1 domain forms an extended filament with the receptor-
CC       binding domain (RBD) at its extremity; in the secretion arrested state
CC       the C-terminus of the RBD domain form a hairpin-like structure as the
CC       FHA-2, PT and CT domains are periplasmic. Upon binding to a target cell
CC       outer membrane receptor a signal is transmitted to activate secretion.
CC       The filament elongates slightly, the rest of CdiA is secreted and the
CC       FHA-2 domain becomes stably associated with the target cell's outer
CC       membrane where it facilitates entry of the toxic CT domain into the
CC       target cell periplasm. From there the toxic CT domain is cleaved and
CC       gains access to the target cell cytoplasm via an inner membrane
CC       protein. {ECO:0000250|UniProtKB:A0A1S4NYE3,
CC       ECO:0000250|UniProtKB:I1WVY3}.
CC   -!- SUBUNIT: Specifically interacts with cognate immunity protein CdiI,
CC       which blocks its tRNA nuclease activity. {ECO:0000269|PubMed:22435733}.
CC   -!- SUBCELLULAR LOCATION: Target cell, target cell cytoplasm
CC       {ECO:0000250|UniProtKB:I1WVY3}. Note=Secreted to the cell surface by
CC       CdiB, its two partner secretion pathway (TPS) partner.
CC       {ECO:0000250|UniProtKB:I1WVY3}.
CC   -!- DOMAIN: The C-terminal domain has toxic activity, which can be
CC       exchanged between N-terminal sections from different toxin molecules.
CC       {ECO:0000269|PubMed:22435733}.
CC   -!- SIMILARITY: Belongs to the CdiA toxin family. {ECO:0000305}.
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DR   EMBL; JQ423913; AFG17278.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9T8G4; -.
DR   SMR; H9T8G4; -.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2310.30; -; 1.
DR   InterPro; IPR038233; Colicin_D/E5_nuclease.
DR   InterPro; IPR021964; Colicin_E5_C.
DR   InterPro; IPR038234; Colicin_E5_C_sf.
DR   InterPro; IPR025157; Hemagglutinin_rpt.
DR   Pfam; PF12106; Colicin_E5; 1.
DR   Pfam; PF13332; Fil_haemagg_2; 3.
DR   SUPFAM; SSF102824; SSF102824; 1.
PE   1: Evidence at protein level;
KW   Endonuclease; Hydrolase; Nuclease; Target cell cytoplasm; Toxin; Virulence.
FT   CHAIN           <1..1269
FT                   /note="tRNA nuclease CdiA"
FT                   /id="PRO_0000429692"
FT   REGION          <1..251
FT                   /note="FHA-2"
FT                   /evidence="ECO:0000305"
FT   REGION          252..991
FT                   /note="Pretoxin (PT) domain"
FT                   /evidence="ECO:0000305"
FT   REGION          317..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1269
FT                   /note="CT domain, has tRNA nuclease activity"
FT                   /evidence="ECO:0000269|PubMed:22435733"
FT   REGION          1124..1155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           992..995
FT                   /note="ELYN CT motif"
FT                   /evidence="ECO:0000305|PubMed:22435733"
FT   COMPBIAS        492..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         1263
FT                   /note="D->A: CT domain not toxic in E.coli."
FT                   /evidence="ECO:0000269|PubMed:22435733"
FT   NON_TER         1
SQ   SEQUENCE   1269 AA;  124362 MW;  683BBBEB48130615 CRC64;
     SLDTTGNVDL TSANVKAGSL DLNAGNKLIL DTATQTTHQV SRDGATSDKT TLGPAANLNV
     AGDASIKTGG DFQQNAGNLN VGGNLNANIG GNWNLGVQQT GEHKVVQRAN GVSDTDLNSA
     TGSTVNVGGK SAIGVGGDLT AQGARLDFGQ GGTVAAKGNV TFGAASTTST INANSSGDQG
     NRSYAETRHG ADQALTGTTV KGGDTLNVVS GKDINVIGST IDLKKGDANL LAAGDVNVGA
     ATETHVYNSR ETHSRSGVVS GTKIASSQDA TSTVANGSLI SADGVSIGSG KDINVQGSTV
     VGTHDVALNA AHDVNITTSQ DTSQSSTTYQ EQHSGLMSGG GLSFSVGNSK LAQQNQSSSV
     TNNASTVGSV DGNLTVNAGN TLHVKGSDLV AGKDVTGTAT NIVVDSATDT THQAQQQQTS
     KSGLTVGLSG SVGDAINNAI SETQAARESA KDSNGRASAL HSIAAAGDVA FGGLGAKALL
     DGAKGPQAPS IGVQVSVGSS HSSMQSSEDQ TIQRGSSINA GGNAKLIATG NGTPKDGNIT
     IAGSNVNAAN VALVANNQVN LVNTTDTDKT QSSNSSSGSS VGVSIGTNGI GVSASMQRAH
     GDGNSDAAIQ NNTHINASQT ATIVSGGDTN VIGANVNANK VVADVGGNLN VASVQDTTVS
     AAHQSSAGGG FTISQTGGGA SFSAQNGHAD GNYAGVKEQA GIQAGSGGFD VTVKGNTDLK
     GAYIGSTADA SKNSLTTGTL TTSDIENHSH YSANSAGFSA GASVGVSTKA VGPSSVSGSG
     GVTPMVFQND SGDQSATTKS AVSAGTINIT KPGEQTQDVA NLNRDTTNLN GTVSKTPDVQ
     KMLSQQADTM NAAQAAGQTV SQAIGLYADY KRDAALDAAD KAYKAGDLAG AQAALNEAKG
     WMEGGASRAE LQMGGGALIG GLGGGSALTA IGGAAGAGTS SLLANQAEKI SKSVGDTTGS
     SLVGNIAANV AATVGGALVG GSAGAAMASN VQLYNAGNDS NNQTSNDVFA SLSKKVAQAI
     AMTADGKAGV WNGMVNVAGV IVNLPNGGPF ASPGDPGYVS LDGLKKPYKS GTSIGPDAEF
     WTPVLATLGL GGKAAAGTGA TTTSADAATV GNGALKTASG DLSAAGNAAR TQPYGNGASA
     SPSPGTATAG SSGANAQLPT ANGGVAAAGT SSATNVGKVV IDGKIGGQLE ARGWTQQEVQ
     AVVNEGPVGT TMDNRSAGKT PDGLPRNDSA SVYGSKSGYV VVNDRTGEVV QVSGKNDPVW
     IPDSRIKWK