CDIA_YERPY
ID CDIA_YERPY Reviewed; 1077 AA.
AC A0A0H3B0B8;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Deoxyribonuclease CdiA {ECO:0000303|PubMed:26449640};
DE Short=DNase CdiA;
DE EC=3.1.-.-;
DE AltName: Full=CdiA-YPIII {ECO:0000303|PubMed:26449640};
DE AltName: Full=Toxin CdiA;
GN Name=cdiA {ECO:0000303|PubMed:26449640}; OrderedLocusNames=YPK_0575;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4ZQU}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 954-1077 IN COMPLEX WITH CDII,
RP FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=YPIII;
RX PubMed=26449640; DOI=10.1016/j.jmb.2015.09.020;
RA Morse R.P., Willett J.L., Johnson P.M., Zheng J., Credali A., Iniguez A.,
RA Nowick J.S., Hayes C.S., Goulding C.W.;
RT "Diversification of beta-augmentation interactions between CDI
RT toxin/immunity proteins.";
RL J. Mol. Biol. 427:3766-3784(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. The C-terminal 123 residues (954-1077) has DNase activity in
CC the presence of Zn(2+), converting supercoiled DNA into open-circular
CC form. Toxic activity is neutralized by coexpression of the cognate
CC immunity protein CdiI-YPIII, but not by non-cognate immunity proteins
CC from other toxin-immunity modules. Expression of the DNase domain as a
CC chimera allows bacteria to attack other non-immune bacteria which
CC become filamentous and have lost DNA staining.
CC {ECO:0000269|PubMed:26449640}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:26449640};
CC -!- SUBUNIT: Interacts with cognate immunity protein CdiI-YPIII, which
CC blocks its toxic DNase activity. {ECO:0000269|PubMed:26449640}.
CC -!- SUBCELLULAR LOCATION: Target cell, target cell cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Encoded in a defective cdi locus that has been
CC inactivated by gene rearragements and deletions.
CC {ECO:0000305|PubMed:26449640}.
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DR EMBL; CP000950; ACA66878.1; -; Genomic_DNA.
DR PDB; 4ZQU; X-ray; 2.09 A; A=954-1077.
DR PDBsum; 4ZQU; -.
DR AlphaFoldDB; A0A0H3B0B8; -.
DR SMR; A0A0H3B0B8; -.
DR EnsemblBacteria; ACA66878; ACA66878; YPK_0575.
DR KEGG; ypy:YPK_0575; -.
DR OMA; LEAQVWD; -.
DR GO; GO:0004530; F:deoxyribonuclease I activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd13444; CDI_toxin_EC869_like; 1.
DR InterPro; IPR033799; CDI_EC869-like.
DR InterPro; IPR025157; Hemagglutinin_rpt.
DR InterPro; IPR006914; VENN_dom.
DR Pfam; PF13332; Fil_haemagg_2; 2.
DR Pfam; PF04829; PT-VENN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Nuclease; Target cell cytoplasm; Toxin; Virulence.
FT CHAIN 1..1077
FT /note="Deoxyribonuclease CdiA"
FT /id="PRO_0000446871"
FT REGION 67..384
FT /note="FHA-2"
FT /evidence="ECO:0000305"
FT REGION 531..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1077
FT /note="DNase activity"
FT MOTIF 781..784
FT /note="VENN CT cleavage motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 531..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 956..962
FT /evidence="ECO:0007829|PDB:4ZQU"
FT TURN 982..984
FT /evidence="ECO:0007829|PDB:4ZQU"
FT STRAND 986..992
FT /evidence="ECO:0007829|PDB:4ZQU"
FT HELIX 995..1000
FT /evidence="ECO:0007829|PDB:4ZQU"
FT HELIX 1006..1019
FT /evidence="ECO:0007829|PDB:4ZQU"
FT STRAND 1023..1026
FT /evidence="ECO:0007829|PDB:4ZQU"
FT STRAND 1029..1032
FT /evidence="ECO:0007829|PDB:4ZQU"
FT TURN 1033..1035
FT /evidence="ECO:0007829|PDB:4ZQU"
FT STRAND 1037..1045
FT /evidence="ECO:0007829|PDB:4ZQU"
FT HELIX 1051..1066
FT /evidence="ECO:0007829|PDB:4ZQU"
FT STRAND 1070..1075
FT /evidence="ECO:0007829|PDB:4ZQU"
SQ SEQUENCE 1077 AA; 110374 MW; 9333B941C681E31D CRC64;
MLSAGSIDVS SQNIAVAGSS VVADKDIRLR AQENLTVSTA QQSESGTQLF EQKKSGLMST
GGIGVFIGTS RQKTTDQTQT VSHIGSTVGS LTGNVRLEAG NQLTLHGSDV VAGKDLALTG
ADVAISAAEN SRSQQYTAES KQSGLTVALS GPVGSAVNTA VTTAKAAREE NTGRLAGLQG
VKAALSGVQA VQAGQLVQAQ GGGITEMVGV SVSLGSQKSS SQQQQEQTQV SGSALTAGNN
LSIKATGGGN AANSGDILIA GSQLKAGGDT RLDAARDVQL LGAANRQKTD GSNSSRGGSI
GVSVGGSGLS VFANANKGQG NERGDGTFWT ETTVDSGGMF SLRSGRDTTL TGAQVSAETV
KADVGRNLTL QSQQDRDNYD AKQSRASGGI SVPVAGGGAA VNLSMSRDRL SSQYDSVQAQ
TGIFAGSGGV DIRVGEHTQL DGAVIASTAA ADKNTLDTGT LGFSDIKNKA VFTVEHQGGS
LSTGGPVGSD LLSNLGGMVL AGLGNGGYAE GTTQAAVSEG TITVRDTENQ QQNVDDLSRD
TGNANGSIGP IFDKEKEQNR LKEVQLIGEI GGQALDIAST QGKIIATHAA NDKMKAVKPE
DIVAAEKQWE KAHPGKAATA EDINQQIYQT AYNQAFNESG FGTGGPVQRG MQAAIAAVQG
LAGGNMGAAL TGASAPYLAG VIKQSTGDNP AANTMAHAVL GAVTAYASGN HALAGAAGAA
TAELMAPTII SALGWDKNTL TEGQKQAVSA LSTLAAGLAG GLTGDSTADA LAGGQAGKNA
VENNYLNSTQ ALTFDKELSD CRKSGGNCQA VIDKWKKVSD EQSVKLDETL KNNPLEAQVW
DKEVAQGGIA ITERPGWLSS LGADVMSSEE AKAYVQQWNG QDLSKIDVNS PGWTKFAAFA
SDPENQVAVA SLGMLGKDLT KAALSYMGRN TSTATVSASS VGMKWGQGNM KQGMPWEDYV
GKTLPVGSRL PPNFKTYDYF DRATGAVVSA KSLDTQTMAK LSNPNQVYSS IKKNIDVTAK
FEKASLSGVT VNSSMITSKE VRLAVPVNTT KAQWTEINRA IEYGKNQGVK VTVTQVK
