CDIA_YERMW
ID CDIA_YERMW Reviewed; 2963 AA.
AC C4SGN7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=tRNA nuclease CdiA {ECO:0000303|PubMed:29923643};
DE Short=tRNase CdiA {ECO:0000303|PubMed:29923643};
DE EC=3.1.-.- {ECO:0000269|PubMed:29923643};
DE AltName: Full=Contact-dependent inhibitor A {ECO:0000303|PubMed:29923643};
DE Short=CdiA-43969 {ECO:0000303|PubMed:29923643};
DE AltName: Full=Toxin CdiA;
DE Flags: Precursor;
GN Name=cdiA {ECO:0000303|PubMed:29923643}; ORFNames=ymoll0001_27200;
OS Yersinia mollaretii (strain ATCC 43969 / DSM 18520 / CIP 103324 / CNY 7263
OS / WAIP 204).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349967;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43969 / DSM 18520 / CIP 103324 / CNY 7263 / WAIP 204;
RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P.,
RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M.,
RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., Willner K.,
RA Zwick M.E.;
RT "Annotation of the Yersinia mollaretii ATCC 43969 genome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 43969 / DSM 18520 / CIP 103324 / CNY 7263 / WAIP 204;
RX PubMed=29923643; DOI=10.1111/mmi.14007;
RA Michalska K., Quan Nhan D., Willett J.L.E., Stols L.M., Eschenfeldt W.H.,
RA Jones A.M., Nguyen J.Y., Koskiniemi S., Low D.A., Goulding C.W.,
RA Joachimiak A., Hayes C.S.;
RT "Functional plasticity of antibacterial EndoU toxins.";
RL Mol. Microbiol. 109:509-527(2018).
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. Targeting of the CT domain (residues 2824-2963) in the absence
CC of immunity protein inhibits cell growth and causes tRNA(UUC-Glu)
CC cleavage in the anticodon loop; expression of cognate immunity protein
CC CdiI-43969 neutralizes growth inhibition and tRNA(UUC-Glu) remains
CC intact, whereas non-cognate immunity proteins do not confer protection
CC from the toxic effects. {ECO:0000269|PubMed:29923643}.
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: Forms a 1:1 complex with cognate immunity protein CdiI.
CC {ECO:0000305|PubMed:29923643}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255}. Target cell, target cell
CC cytoplasm {ECO:0000305|PubMed:29923643}. Note=Secreted to the cell
CC surface by CdiB, its two partner secretion pathway (TPS) partner.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CdiA toxin
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the bacterial EndoU
CC family. {ECO:0000305}.
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DR EMBL; AALD02000043; EEQ09309.1; -; Genomic_DNA.
DR RefSeq; WP_004876812.1; NZ_CP054043.1.
DR SMR; C4SGN7; -.
DR EnsemblBacteria; EEQ09309; EEQ09309; ymoll0001_27200.
DR GeneID; 57919904; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR010069; CdiA_FHA1_rpt.
DR InterPro; IPR029501; EndoU_bac.
DR InterPro; IPR008619; Filamentous_hemagglutn_rpt.
DR InterPro; IPR008638; Filamn_hemagglutn_N.
DR InterPro; IPR025157; Hemagglutinin_rpt.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR006914; VENN_dom.
DR Pfam; PF14436; EndoU_bacteria; 1.
DR Pfam; PF05594; Fil_haemagg; 9.
DR Pfam; PF13332; Fil_haemagg_2; 5.
DR Pfam; PF05860; Haemagg_act; 1.
DR Pfam; PF04829; PT-VENN; 1.
DR SMART; SM00912; Haemagg_act; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01901; adhes_NPXG; 1.
DR TIGRFAMs; TIGR01731; fil_hemag_20aa; 7.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Nuclease; Secreted; Signal; Target cell cytoplasm;
KW Toxin; Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..2963
FT /note="tRNA nuclease CdiA"
FT /evidence="ECO:0000255"
FT /id="PRO_0000446870"
FT REGION 35..320
FT /note="Two-partner system transport domain (TPS)"
FT /evidence="ECO:0000250|UniProtKB:Q3YL96"
FT REGION 573..1074
FT /note="FHA-1"
FT /evidence="ECO:0000305"
FT REGION 1075..1342
FT /note="Receptor binding domain (RBD)"
FT /evidence="ECO:0000250|UniProtKB:A0A1S4NYE3"
FT REGION 1343..1528
FT /note="YP domain"
FT /evidence="ECO:0000250|UniProtKB:Q3YL96"
FT REGION 1529..1751
FT /note="Periplasmic FHA-1 repeat (pFR)"
FT /evidence="ECO:0000305"
FT REGION 1759..1787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..2314
FT /note="FHA-2"
FT /evidence="ECO:0000305"
FT REGION 1992..2012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2694..2963
FT /note="C-terminal effector domain (CT)"
FT /evidence="ECO:0000269|PubMed:29923643"
FT MOTIF 2694..2697
FT /note="VEDN CT cleavage motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 1771..1787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2963 AA; 308750 MW; 43A14562136B6E59 CRC64;
MIPIYLRQKL ISYALIYLVA IQPIMPVMAA GIDVAQGSTA LDKAGNGVPV VNIAPPNSAG
VSHNVYNQFN VGSEGVILNN ATDRLTQTQL GGLIQSNANL NGKAAGAIIN EVVSANRSQL
NGYLEVGGKA AAVMVANPYG ITCDGCGFIN TPNVTLTTGK PMMDTNGKLQ SLDVTQGAIS
IQGKGLDASQ SSALSLISRA NEINAQIHAQ DLTVIAGSNR VDSAGHVSER QGQGDVPQVS
IDTGALGGMY ANRIRLVSSE KGVGVNLGNL NARQGDIQLD SKGKLTVNNA VAHGDIIASA
DQLHLQGHQR AQGNITLNSH GESRLDNATL LAGDTLAVKA GGKITSKESQ LNAGVDSAGN
IGEKGTVSLQ GSELALQQSH VAAAAVSVVS SGDIVQDKES SLTARQLKLS GQHLELAGQL
AANNDLSITG QSLRGSKTAS VGSQKNITFN LAGDSEWAGQ MVAGNDLIFS GQSLTNHGQL
LAANQMHFEG LGLDNQGQIL AADINIAVHR LNNQGQLQGD KSLLLTADSL VQSTRGTMNS
GRALTLRAAE MDISGDLQSQ ILDVKGDNWH NHGNVVAQEH AQLRLGHTID NRGVLVSAGD
MDLSFNQLSN QGRILGAELA LSGKNISNSG QLVGKQQLSL QLDEGYQGTS SGELKSDGLL
SVTADEINNQ GHWESGSLNT TAQQLTNNGK VLSVGSQNIN LSGSLTNQQL GQFLTDGEFI
IVAEQVINSG LLQGNQAVTL NGLKQYQGGT GSQLLTKGVG EIHSDSVNNA GLIQAGSLSL
TGEVLDNTGT LSGLSTLHID SHNEIINQAR GQLLSDNTIK LDSEQLVNNG LMQGTELVLA
SQHLTNNGTL LGLTYLELQA VNLTNSSAGK ILSGQDLHFT TSHLQQNGQW TALRDLTGEI
KGALDFSGAM AAGKQLSLQV DGDFNQRGNL QGNDVSITSR GVITNSGQLA AGSGSLALNG
AAINQEQSGS LQSGGQISLT SRGDINNRGF VGAAGDLLLQ AIGAVNNTSL LYAGGSMRLL
ADAIYNVRGD ILAGNHLWMQ RDNAGNSNRE IINSSGNIET QQGDMVLNTA SLLNRRDGFS
VTEKTGAVNS GGIANVGATN ILISSGYFKP GEVTHYSKTV TGGGHHGNVS TVNLLGLVPS
ARKQKLSTSS SIVTVDSPYD VGRIVAGRDI NISANTLVNQ ASQMSAGRNA LLQGQSLNNQ
SYQSGTLTQY LVYTNTRDTN PEYNLFEFKL SGSPTYEISN DGQLYQGVIQ AVGSVSANFT
QNLSNTSVKP NIGSIVHQVT QPSLTATTVP SELATKPNSG AAQVAPDSNN GDLVALYNQS
GTALTFGLGT DGKPLTRAQL SDYPLPDSNN GLFVVNSEPG SRYLISTNPT LEKLGNVDST
LLSGLQAMLG RQPQTSVAIE RNPQWTQQDN FLGSDYLLKK INLDAEHDYR FLGDAAFDTR
YINNAVLSQT GQRYLNGVGS DLSQMQYLLD NAAQSQKKLD LKLGVSLTPE QVAQLSHSIV
WWENINVNGQ TVLAPKLYLA KAEQAHLQGS VISGNKVELN AGSVTNSGVL KGVELLAIAS
QDTITNEKGG LLTSEGALNL TALNNISNLS SSISGDRVAI TSQNGDIINQ TQTRQWSADQ
SRQPGYWSGI KTQSMTQTEV GETAAITAGK ALTLAAGNNI AITGAKVTAA GDIGIQAAHD
INIIANDLYS AQQQTLGRNR NIELNEQHES QSSHVSAGGT LTAHAGRDIT LSASHLGADG
NATLQAERDV NLLVQEKSTR NQHIDSEDKT TGYTRSTLSS GGDLTASAGR DINSQAAAVT
AENTLALNAG RDINLNAQES RQYNESHGKN YKRVDEAIRQ QGTELASGKG TQVHAGQDIN
LHAASISAKG DLALQAGRDI AVNSATESDY HFFEEKKTKK KLVSKTTIHN VEEDFATTEK
SSALVGNNVS LSAGNNLIVK GSSVVGDGTV VLKADNNVDI VAATEQQSSY RLNEKKTSGM
FSGGGLGVTL GSKSSRQQIN QEGSKQSESA SAVGSTAGNV SILAGAQAHI SGSDVIAGKD
LNVIAGTIKV DPGNDVLKRR QIYEQKQSGL TLSLSSPFTD ALLAINSKLK QASDAGSDKL
SALYGAQAAR EAWVGVDGTM DMMASKPGGP AADPGASIKL QLSVGASHSK STSELAQNQT
RGSSLTAGDN LTMVASGDHE QSGDLSVVGS GVTGNKVTLV AKNDVLLAAA SNNSEQTSRD
SSSGWNAGVH LSLGKETGIG IAANGFMSKG NSDGKTTDYA NARINAKEAL AINSGRDTVL
SGAQVLGDKI TAEIGRDLTI SSLQDSDNYN SIQKDASAGF SFTFGPSGGG SASFSLGKTK
IESKYASVGD QSGFFAGSKG FDLNVGNHTQ LNGGVLASTA GAQDNLLSTG TLGWGDIHNQ
AEYKATSTRI GYSTDAPMPT LGMANAHGSA SGTTRSAVAS GEIEIRNQGE QQQDVTTLSR
DTDSANGRID KIFDESKVKD QMAFTQGVTQ LATQLVGDVS SWNMKQAERS AAEKLEKDPK
YQNATREKRQ EMIYASADYK AAQESFGIGS SFWTAGMAVS AALTGLAGNA DIGSISSAAV
APYLAGQIKK YTTDKDDKVN KTINILAHAI LGGIVAQMQG NSATAGALGG GGGELAARIY
MDQVHPGKKV SDLSEADKKI VSAIGTLTAG ILGGLSTDSS TGLITGAQAG KNAVEDNNLS
FGKGMADIGM SQTSLGVSML RNGTSPDEVS AALVKNSLGQ TPEGQDPIRG LLTAWAEFFG
VPVTALIANG PMTVERAAEI VSSGVPTSEA KLIQYTAAKA FLAVAKNLPQ GTTLVSTPEG
ISFRIDQPKH LSSVDGFTQK AGISGGHNAD AFYEAAKQYD VKILSETSTG AKGITEVKYQ
IPTKDRAGNL TGGYKPAVET KTIYDPNVFT DQKILELGQQ AAAKGYKDAM ASKSGQASAT
VDGVSFRIYV DKDTGRVRNF HPN
