CDIA_DICD3
ID CDIA_DICD3 Reviewed; 3326 AA.
AC E0SDG8;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Deoxyribonuclease CdiA {ECO:0000303|PubMed:21085179};
DE Short=DNase CdiA;
DE EC=3.1.-.-;
DE AltName: Full=CdiA-Dd3937;
DE AltName: Full=Toxin CdiA;
GN Name=cdiA {ECO:0000303|PubMed:21085179}; Synonyms=hecA2;
GN OrderedLocusNames=Dda3937_02098;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [2]
RP FUNCTION, STRAIN SPECIFICITY, INTERACTION WITH CDII, SUBUNIT, AND DOMAIN.
RC STRAIN=3937;
RX PubMed=21085179; DOI=10.1038/nature09490;
RA Aoki S.K., Diner E.J., de Roodenbeke C.T., Burgess B.R., Poole S.J.,
RA Braaten B.A., Jones A.M., Webb J.S., Hayes C.S., Cotter P.A., Low D.A.;
RT "A widespread family of polymorphic contact-dependent toxin delivery
RT systems in bacteria.";
RL Nature 468:439-442(2010).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=3937;
RX PubMed=23469034; DOI=10.1371/journal.pone.0057609;
RA Webb J.S., Nikolakakis K.C., Willett J.L., Aoki S.K., Hayes C.S., Low D.A.;
RT "Delivery of CdiA nuclease toxins into target cells during contact-
RT dependent growth inhibition.";
RL PLoS ONE 8:E57609-E57609(2013).
RN [4]
RP FUNCTION, REQUIRES PMF FOR TRANSLOCATION, AND SUBCELLULAR LOCATION.
RC STRAIN=3937;
RX PubMed=25174572; DOI=10.1111/mmi.12779;
RA Ruhe Z.C., Nguyen J.Y., Beck C.M., Low D.A., Hayes C.S.;
RT "The proton-motive force is required for translocation of CDI toxins across
RT the inner membrane of target bacteria.";
RL Mol. Microbiol. 94:466-481(2014).
RN [5]
RP RECEPTOR FOR ENTRY INTO TARGET CELL CYTOPLASM.
RC STRAIN=3937;
RX PubMed=26305955; DOI=10.1073/pnas.1512124112;
RA Willett J.L., Gucinski G.C., Fatherree J.P., Low D.A., Hayes C.S.;
RT "Contact-dependent growth inhibition toxins exploit multiple independent
RT cell-entry pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11341-11346(2015).
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. CDI is neutralized by its cognate immunity protein CdiI, but
CC not by non-cognate CdiI from other bacteria. The C-terminal domain (CT)
CC has strong DNase activity; this activity is inhibited by cognate CdiI.
CC {ECO:0000269|PubMed:21085179, ECO:0000269|PubMed:23469034,
CC ECO:0000269|PubMed:25174572}.
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 and YP domains form a hairpin-like structure
CC as the FHA-2, PT and CT domains are periplasmic. The YP domain is
CC probably responsible for this arrest at the point where it re-enters
CC the host cell periplasm. Upon binding to a target cell outer membrane
CC receptor a signal is transmitted to activate secretion. The filament
CC elongates slightly, the rest of CdiA is secreted and the FHA-2 domain
CC becomes stably associated with the target cell's outer membrane where
CC it facilitates entry of the toxic CT domain into the target cell
CC periplasm. From there the toxic CT domain is cleaved and gains access
CC to the target cell cytoplasm via an inner membrane protein.
CC {ECO:0000305}.
CC -!- SUBUNIT: The C-terminal (CT) domain interacts with cognate CdiI but not
CC non-cognate CdiI from E.coli strain 536 / UPEC.
CC {ECO:0000269|PubMed:21085179}.
CC -!- SUBCELLULAR LOCATION: Target cell, target cell cytoplasm
CC {ECO:0000269|PubMed:23469034, ECO:0000269|PubMed:25174572}. Note=In
CC mixing experiments where target cells lack cdiI the DNase activity can
CC be detected in target cells as a loss of DAPI staining
CC (PubMed:23469034). Secreted to the cell surface by CdiB, its two
CC partner secretion pathway (TPS) partner (Probable). Toxin translocation
CC into the target cell depends on the proton motive force of the target
CC cell, but not on tolA or tonB (PubMed:25174572).
CC {ECO:0000269|PubMed:23469034, ECO:0000269|PubMed:25174572,
CC ECO:0000305}.
CC -!- DOMAIN: The CDI activity resides in the approximately 260 residue C-
CC terminal (CT) domain; exchanging the C-terminal (CT) domain and cdiI
CC gene between different strains confers resistance within cognate but
CC not non-cognate systems (i.e. CdiI-3937 neutralizes CdiA-CT from 3937
CC but not CdiA-CT from E.coli strain 536 / UPEC or EC93 or Y.pestis
CC CO92). {ECO:0000269|PubMed:21085179}.
CC -!- MISCELLANEOUS: There are 2 cdiBAI loci in this strain, this is locus 2.
CC {ECO:0000303|PubMed:21085179}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CdiA toxin
CC family. {ECO:0000305}.
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DR EMBL; CP002038; ADM98660.1; -; Genomic_DNA.
DR STRING; 198628.Dda3937_02098; -.
DR EnsemblBacteria; ADM98660; ADM98660; Dda3937_02098.
DR KEGG; ddd:Dda3937_02098; -.
DR PATRIC; fig|198628.6.peg.2438; -.
DR eggNOG; COG3210; Bacteria.
DR HOGENOM; CLU_000043_2_2_6; -.
DR OMA; NVADANL; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0004536; F:deoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR010069; CdiA_FHA1_rpt.
DR InterPro; IPR008619; Filamentous_hemagglutn_rpt.
DR InterPro; IPR025157; Hemagglutinin_rpt.
DR InterPro; IPR006914; VENN_dom.
DR Pfam; PF05594; Fil_haemagg; 8.
DR Pfam; PF13332; Fil_haemagg_2; 4.
DR Pfam; PF04829; PT-VENN; 1.
DR TIGRFAMs; TIGR01731; fil_hemag_20aa; 23.
PE 1: Evidence at protein level;
KW Hydrolase; Nuclease; Reference proteome; Target cell cytoplasm; Toxin;
KW Transferase; Virulence.
FT CHAIN 1..3326
FT /note="Deoxyribonuclease CdiA"
FT /id="PRO_0000432086"
FT REGION 36..342
FT /note="Two-partner system transport domain (TPS)"
FT /evidence="ECO:0000250|UniProtKB:Q3YL96"
FT REGION 343..1396
FT /note="FHA-1"
FT /evidence="ECO:0000305"
FT REGION 1397..1765
FT /note="Receptor binding domain (RBD)"
FT /evidence="ECO:0000250|UniProtKB:A0A1S4NYE3"
FT REGION 1766..1951
FT /note="YP domain"
FT /evidence="ECO:0000250|UniProtKB:Q3YL96"
FT REGION 1959..2097
FT /note="Periplasmic FHA-1 repeat (pFR)"
FT /evidence="ECO:0000305"
FT REGION 2125..2660
FT /note="FHA-2"
FT /evidence="ECO:0000305"
FT REGION 3060..3326
FT /note="CT domain"
FT /evidence="ECO:0000305|PubMed:21085179"
FT MOTIF 3060..3063
FT /note="VENN CT cleavage motif"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3326 AA; 338537 MW; 789E8CCBE375838B CRC64;
MAADTLMVTG AWLSNSGTLQ GRQSVGLAVG RDFSQTADGV LTSGGTVTVT AGGVATAGAL
TAQGLALTAG RWRHQGAVTL GGDGRLVLDE LDNGGTLRAG GAWDMQAAAL SNGGTLQGGR
LALTLSGAAV NRGTLAGERV TLTADSLDNG GTLLGMDALT LAIAGTARNQ ASGQWLSQGE
SRLTAGTLDN QGQWQGDSLS VTADRIRNAG QLLGLSALTL TADGTLTNTA TGTLLTQGAA
VLRAATVDND GEWQAGRLRL TADSLRNGGR IQSDGALDVA LSPAGVLTNT GTLAANGDTT
LTPGGLDNRG AVSVRGDLTV TGTDLDNAGQ LAARGALTLT GSYAGAGSLY SDAALTLRGT
TLANDGGRWQ GQTVDIGGGP LTNDGNITGL DSLTVTTTGA LTNRGRLAGQ TLGITADALD
NAGTLLGVDA LTLAIAGTAR NQTSGQWLSN GAGRLTAGTL DNRGQWQGDS LDATADRLDN
AGTLLGLSAM TLTVNGALTN TGRLLTQGAA VLSAATADND GEWQTGSLWL TADSLRNGGQ
IHSDGEVRIT LPTADGDPLR PTLRAARQLA QDVEAIGAGR LSNTGVLTAG GDGRITGRGL
DNAGTLAAGG ALTLAAGDLT NAGRLESRTL SLTGDSLDNG GTLLAEQGGE LTLGGGLHVG
ADGRLLSNGD WQVQAGTVTS LGQWQGKTLL LSAASLDNGG ALLATDAVTL TLTQGYTGGA
GSQVLGSGAV TLTADTVTQQ GDIGGDRLAL TTGTLTNGGR LVGLSQLDVT SRGQLTNRAT
GSLLGNGTAG VTAATLDNAG SVQADTLTLT ADTVTNAGRM QGTSALTLNG VSRYTGTDGS
QLLSGGTATL AIDNADNAGL WQAGELRFRG ASLTSRGQIT GLDSLTVDAA SLTSTGQLTT
RGLATLRGQR FDNGGTLTAL GGFTARFSDS VTNQGGGQLL SGGTGSLTTG TLVNRGRWQS
DRLTLTADTL RNPGTLLGLD DGNIQLTGAY VGEAGSQVGG NGALSLSAAT IDQAGQWQAR
DVTLRATRLR NQGSITGSGQ LTATLDEQLE NLAGATLLGG TVWLGGATVS NGGQIQGRSG
LTVQGGTLLD NQGGGQLLSG GQLALGATQL TNAGWVQGQD LTLTTAQLDN SGTLQAQSGL
TLHLPQWTNR GTVQAGQLDI TTDGALDNRG TLLGLTRLAL QAASLNNADG ARLYSAGGLQ
LRTGQLTQDG QLAALGDLRA DIGTPFTFTR TLAAGGQLTL AVTGDLVQAG TLQGHGVTVT
STGTLTQQGR IVAGGGNSTL SAAAISQTES GSIQGGGPLS LRATGNIVNR GFVGTAGDLL
VQAGGVMENG SLLYGGGNLQ LLSAALVNRF GNILAGGSLW IQRDAAGNAS DSVLNSSGTI
ETQRGDITVR TGTLTNQREG LVVTESGSTA ADMPDWVGGT TIYIPVERFE VIKDYLVYSF
EHTPGAGSDS PTTYNYFYPF PLSHVSKQEF SASSKIVNIE SKGGSSLIHS AGDINIFSSV
LVNDASIIAS EKNILMNGGV LKNSSYQSGV MSESLIYEYE RDDKDDFLPY IEWLWEKTKR
EEGVSDYDYW EYLSGYNIHA YNRNILTNDR FKYVLKDRQI IFTPGQTYAA TIQAGGAITA
NFSQNISNTN LQPGSGGFMP AMATPTLAGV NALGPVGAQA DRGLNGGTAG NVSGSTLSGA
GNGVALAGQA GRLNAGYSAV TRDNTASSGS ALNPVGIPAG PGTAGGAPVA GASLTPVAPG
ALALSDLQAA LAQGLQQLGS PSLTDYPLPT SQSGLFVADT AGDSRYLIRT NPTLSQLGQV
DNALFGDLRG LLGQTPGTTA PVERSPTLTD PTQVLGSSYL LGKLNLDAEH DYRFLGDAAF
DTRYISNAVL SQTGQRYLNG VGSELAQMQQ LMDNAAAEKS RLNLQLGVSL TPEQVAGLSH
SLVWWENITV GGQTVLAPKL YLAQADKTNL QGSRIVANSV SLSAGGDIDN RGSTVTAQDA
LAVASGGNLT NSEGGLLNAG GALNLVALGN LTNSSATIQG NTVTLASVGG DIVNTTTTDQ
WQTAARDGRG RGSLTRTDIG QAGLISAQGG LTLQAGHDIA LNGAQLSAGG PLQLAAGNDI
RLTALSTVTD TVRQDGGATT ERRGQGLVQS TVASGGDLSL SAGRDLSGTA AQLSAAGTLA
LSAGRDLSLL SASEEQFSSN AWKRHLDWQQ TVTQQGTVLN AGEGLSLRAG QDLTLQGAQA
ETRGALTAQA GRDLSLLSAT ESRHDFFEET TVKKGFLSKT TTHTLRETQQ TTEKGTLLSA
GSVALTAGHD IGVQGSAVAA DGEVTLTAGN DITTAASVET YRNYEEQSRK KSGVFSGGGI
GFTIGSTSLR QTLESAGTTQ SQSVSTLGST GGSVRLNAGQ AVSMAATDVI AARDIQVTGN
SVTIDPGYDT RKQSRQMEQK TAGLTVTLSG VVGSALNSAV QTVQAVREQS DSRLQALQGM
KAALSGYQAY QGTQIDTNNQ GASSFVGISV SLGAQRSSSS QTSEQSQSFA STLNAGHDIS
VVARQGDITA VGSQLKAANN VELNASRAIN LLSARNTESM TGSNSSSGGN IGVSFGLSNS
GAGFSVFANV NAAKGRELGN GNSWSETTVD AGQQIALTSG GDTRLTGAQV SGERIVANVG
GDLLLKSQQD SNRYDSKQTS VSAGGSFTFG SMTGSGYLSA SQDKMHSSFD SVQQQTGLFA
GKGGYDISVG NHTQLDGAVI GSTAGADKNR LDTGTLGFSN IDNRAEFSVS HSGIGLSASP
SLSMSDMLKS AALTAPSALM SMGRGGNAGS TTYAAVSDGA LIIRNQAGQQ QDIAGLSREV
EHANNALSPI FDKEKEQKRL QTAQMVGELG AQVMDVIRTE GEIRAVRAAE AKGDVKRPPD
NASEKDWDKY KKDLTETPAY KAVMQSYGTG SDLQRATQAA TAAIQALAGG GNLQQALAGA
SAPYLAQLVK GVTMPADESK ATASDIAANA MGHALMGAVV AQLSGKDAVA GAVGAAGGEL
TARLLIMKEL YSGRDTSDLT EAEKQSVSAL ASLAAGLASG IASGNTTGAA TGAQAGRNAV
ENNSLGDIAQ AQSEGKTLEQ NAGEYVEAEN ERYKKENCAG LSAEACSVKM YEERREELKE
TLSTGADFVP VIGDIKSFAE AQSALDYLAA AVGLIPGAGD AAGKAIKAAE TALKKGELAE
ASKLINKASD EIQAVKPLDV GSYKELKDRA VVGDGLEHDH IPSFAALRTA KENELGRKLT
PAEEKTLYQN ATAVEVPKDV HRAGPTYGGK NTAAQVQQDA LDLCGAVCRD TDALRTNMIE
RGYEPALVDD AVKKIIDRNR QIGVIK
