CDIA1_ECO5C
ID CDIA1_ECO5C Reviewed; 3209 AA.
AC B3BM48;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=tRNA nuclease CdiA {ECO:0000303|PubMed:25174572};
DE Short=tRNase CdiA;
DE EC=3.1.-.-;
DE AltName: Full=CdiA-EC869 {ECO:0000303|PubMed:25174572};
DE AltName: Full=Toxin CdiA;
DE Flags: Precursor;
GN Name=cdiA1 {ECO:0000303|PubMed:25174572}; ORFNames=ECH7EC869_5848;
OS Escherichia coli O157:H7 (strain EC869).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=478008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC869;
RX PubMed=21421787; DOI=10.1128/aem.02554-10;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genome signatures of Escherichia coli O157:H7 isolates from the bovine
RT host reservoir.";
RL Appl. Environ. Microbiol. 77:2916-2925(2011).
RN [2]
RP FUNCTION, REQUIRES PMF FOR TRANSLOCATION, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=EC869;
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 [3]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=EC869;
RX PubMed=28223500; DOI=10.1073/pnas.1619273114;
RA Jones A.M., Garza-Sanchez F., So J., Hayes C.S., Low D.A.;
RT "Activation of contact-dependent antibacterial tRNase toxins by translation
RT elongation factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1951-E1957(2017).
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 domain (CT) endolytically cleaves tRNA(CUG-Gln)
CC (PubMed:25174572, PubMed:28223500). Cleaves tRNA(CUG-Gln) in the
CC acceptor stem between C70 and A71. Also cleaves tRNA(GUU-Asn). Requires
CC wild-type EF-Tu (tufA) and GTP for activity in vivo and in vitro; EF-Ts
CC (tsf) stimulates the tRNase but is not absolutely required in vitro
CC (PubMed:28223500). {ECO:0000269|PubMed:25174572,
CC ECO:0000269|PubMed:28223500}.
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: Probably interacts with cognate immunity protein CdiI1
CC (Probable). Forms a contact-dependent growth inhibition complex of EF-
CC Tu, CdiA-CT-EC869 and CdiI-EC869 as well as a GTP, EF-Tu, CdiA-CT-EC869
CC complex; EF-Ts does not stably associate with either complex
CC (PubMed:28223500). {ECO:0000269|PubMed:28223500,
CC ECO:0000305|PubMed:25174572}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell, target cell
CC cytoplasm {ECO:0000305|PubMed:25174572}. Note=Secreted to the cell
CC surface by CdiB, its two partner secretion pathway (TPS) partner
CC (Probable). Toxin translocation into the target cell depends on the
CC proton motive force (pmf) of the target cell, but not on tolA or tonB.
CC The pmf is probably required for translocation across the target cell
CC inner membrane from its periplasm. {ECO:0000269|PubMed:25174572,
CC ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CdiA toxin
CC family. {ECO:0000305}.
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DR EMBL; ABHU01000020; EDU89581.1; -; Genomic_DNA.
DR RefSeq; WP_001075571.1; NZ_ABHU01000020.1.
DR SMR; B3BM48; -.
DR PRIDE; B3BM48; -.
DR EnsemblBacteria; EDU89581; EDU89581; ECH7EC869_5848.
DR Proteomes; UP000004641; Unassembled WGS sequence.
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; 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; PF13332; Fil_haemagg_2; 4.
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; 20.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Nuclease; Repeat; Secreted; Signal;
KW Target cell cytoplasm; Toxin; Virulence.
FT SIGNAL 1..32
FT /evidence="ECO:0000305"
FT CHAIN 33..3209
FT /note="tRNA nuclease CdiA"
FT /id="PRO_0000432087"
FT REGION 36..322
FT /note="Two-partner system transport domain (TPS)"
FT /evidence="ECO:0000250|UniProtKB:Q3YL96"
FT REGION 351..1394
FT /note="FHA-1"
FT /evidence="ECO:0000305"
FT REGION 1395..1651
FT /note="Receptor binding domain (RBD)"
FT /evidence="ECO:0000250|UniProtKB:A0A1S4NYE3"
FT REGION 1652..1836
FT /note="YP domain"
FT /evidence="ECO:0000250|UniProtKB:Q3YL96"
FT REGION 1837..1875
FT /note="Periplasmic FHA-1 repeat (pFR)"
FT /evidence="ECO:0000305"
FT REGION 1946..2542
FT /note="FHA-2"
FT /evidence="ECO:0000305"
FT REGION 2221..2246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2355..2392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2925..3209
FT /note="C-terminal effector domain (CT); has tRNA(CUG-Gln)
FT endonuclease activity"
FT /evidence="ECO:0000269|PubMed:25174572,
FT ECO:0000269|PubMed:28223500"
FT COMPBIAS 2232..2246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2357..2392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3209 AA; 327167 MW; 6B48C0A482CC2E6D CRC64;
MNQPPVHFTY RLLSYLVSAI IAGQPLLPAV GAVITPQNGA GMDKAANGVP VVNIATPNGA
GISHNRFTDY NVGKEGLILN NATGKLNPTQ LGGLIQNNPN LKAGGEAKGI INEVTGGNRS
LLQGYTEVAG KAANVMVANP YGITCDGCGF INTPHATLTT GRPVMNADGS LQALEVTEGS
ITINGAGLDG TRSDAVSIIA RATEVNAALH AKDLTVTAGA NRITADGRVS ALKGEGDVPK
VAVDTGALGG MYARRIHLTS TESGVGVNLG NLYAREGDII LNSAGKLVLK NSLAGGNTTV
TGTDVSLSGD NKAGGNLSVT GTTGLTLNQS RLVTDKNLVL SSSGQIVQNG GELTAGQNAM
LSAQHLNQTS GTVNAAENVT LTTTDDTTLK GRSIAGKTLT VSSGSLNNGG TLVAGRDATV
KTGTFSNTGT VQGNGLKVTA TDLTSTGSIK SGSTLDISAR NATLSGDAGA KDSARVTVSG
TLENRGRLVS DDVLTLSATQ INNSGTLSGA KELVASADTL TTTEKSVTHS DGNLMLNSAS
STLAGETSAG STVSVKGNSL KTTATAQTQG NSVSVDVQNA QLDGTQAARD ILTLNASEKL
THSGKSSAPS LSLSAPELTS SGVLVGSALN TQSQTLTNSG LLQGKASLTV NTQRLDNQQN
GTLYSAADLT LDIPDIRNSG LITGDNGLTL NTASLSNPGK IIADTLNVRA TTLDGDGLLQ
GAGALALAGD TLSQGRNGRW LTAGDLSLRG KTLHTAGTTQ GQNLTVQADN WANSGSVLAT
GNLTASATGQ LTSTGDIMSQ GDTTLNAATT DNRGSLLSAG TLSLDGNSLD NRGTVQGDHV
TIRQNSVTNS GTFTGIAALT LAARMVSPQP ALMNNGGSLL TSGDLTITAG SITSSGHWQG
KRVLITADSL ANSGAIQAAD SLTARLTGEL VSAAGSKVTS NGEMALSALN LSNSGQWIAK
NLTLKANSLT SAGDITGVDA LTLTVNQTLN NHASGKLLSA GVLTLKADSV TNDGQLQGNA
TTITAGQLTN GGHLQGETLT LTASGGVNNR SGGVLMSRNA LNVSTATLSN QGTIQGGGGV
SLNATDRLQN DGKILSGSNL TLTAQVLANT GSGLVQAATL LLDVVNTVNG GRVLATGSAD
VKGTTLNNTG TLQGADLLVN YHTFSNSGTL LGTSGLGVKG SSLLQNGTGR LYSAGNLLLD
AQDFSGQGQV VATGDVTLKL IAALTNHGTL AAGKTLSVTS QNAITNGGVM QGDAMVLGAG
EAFTNNGMLT AGKGNSVFSA QRLFLNAPGS LQAGGDVSLN SRSDITISGF TGTAGSLTMN
VAGTLLNSAL IYAGNNLKLF TDRLHNQHGD ILAGNSLWVQ KDSSGTANSE IINRSGNIET
TRGDITMNTA HLLNSWDAIS ASHEVIPGSS HGVISPVPEN NRWWGVVRHD GVEYLAVYWG
EGATVPDEYR IRTGDTETVT VSASGHAARI SGGADMHIRA GRLDNEASFI LAGGSMTLSG
DTLNNQGWQE GTTGKETVWR LASGSLPKAW FTEPWYKVYR QVSTDATEAS GTSPAGQYRA
VISAASDVSA SFATDTGNTT VMPRAGGAGN TITVPSLNSL TPPTVSQGVS GEALLNESGT
GITGPVWNDA LPDTLKDIPG ALSLSGASVS SYPLPSGNNG YFVPSTDPDS PYLITVNPKL
DGLGKVDSSL FAGLYDLLRM QPGQAPRETD PAYTDEKQFL GSSYILDRLG LKPEKDYRFL
GDAAFDTRYV SNVILNQTGS RYINGTGSDL AQMKYLMDSA AAQQKALGLT FGVSLTAGQV
AQLTRSILWW ESVTINGQTV MVPKLYLSPE DITLHNGSVI SGNNVQLAGG NITNSGGSIN
AQNDLLLDST GSIDNLNAGL INAGGALNLK AIGDIGNISS VISGKTVSLE SATGNISNLT
RTEQWAMNNG YNHFSGTDTG PLAAVRATDS LFMGAAGDIS ITGAAVSAGD SVLLSAGNDL
NMNAIQAGER RRYGGSGWYE THAVAPTVTA GNSLMLSAGR DVNSQAAGIM AENSMDIRAG
RDVNMAAEST GTGDHDSTFS MKTVHDSVRQ QGTDMTSGGD ITVTAGRDIT SVATAVTAKG
DIRVNAGHDI VLGTATESDY HYSESGETRN RLLSHQTTRT ITEDSVTREK GSLLSGNRVT
VDAGDNLTVE GSDVVADRDV SLAAGNHVDV LAATSTDTSW RFKETKKSGL MGTGGIGFTI
GSSKTTHDRR EAGTTQSQSA STIGSTAGNV SITAGKQAHI SGSDVIANRD ISITGDSVVV
DPGHDRRTVD EKFEQKKSGL TVALSGTVGS AINNAVTSAQ ETKESSDSRL KALQATKTAL
SGVQAGQAAA MATATGDPNA TGVSLSLTTQ KSKSQQHSES DTVSGSTLNA GNNLSVVATG
KNRGDNRGDI VIAGSQLKAG GNTSLDAAND VLLSGAANTQ KTTGRNSSSG GGVGVSIGAG
GNGAGISVFA SVNAAKGSEK GNGTEWTETT IDSGKTVTIN SGRDTVLNGA QVNGNRIIAD
VGHDLLISSQ QDTSKYDSKQ TSVAAGGSFT FGSMTGSGYI AASRDKMKSR FDSVAEQTGM
FAGDGGFDIT VGRHTQLDGA VIASTATPDK NHLDTGTLGF SDLHNEADYK VSHSGISLSG
GGSFGDKFQG NMPGGMISAG GHSGHAEGTT QAAVAEGTIT IRDRDNQKQN LANLSRDPVH
ANDSISPIFD KEKEQRRLQT VGLISDIGSQ VADIARTQGE LNALKAAKEA TGETLPANAT
EKQRQEYLAK LRDTQAYRNE MAKYGTGSEI QRGIQAATAA LQGLAGGNLA GALAGASAPE
LAHLLKSTEK YPAVNAIAHA ILGGAAAAMQ GNNVAAGAAG AATGELAARA IAGMLYPGVK
QSDLSEEQKQ TISTLATVSA GLAGGLTGNS TASAAVGAQS GKNAVENNYL SKAQKAQKAD
ELAKCQTAAC KAQTEAKWTA IDLGQDGSFA AGMIAGVPAG LYDAVDSIVK AGSNPTETLE
AMKALFNSGD ILGSLSDAVK QSYIDRIDRM EAEYQKAGTS GSFNAGVEGG KLITDIAGLL
AGGVGVVKGG AVLTEKVVAK VVGKSESAAA KVGTDIVKTG TVFDSIKATQ PAIPGTSIPK
SFELHVNGQT VWVNPNATKH MGEYLTRNGL SHSTAEGSQA MLTSLQSAVK DAFSQGLKFN
EKMQVGRWEL VFSQRSSDPY PVLKHALYK
