CDIA_YERPE
ID CDIA_YERPE Reviewed; 3295 AA.
AC Q7CGD9;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Toxin CdiA {ECO:0000305|PubMed:21085179};
GN Name=cdiA {ECO:0000303|PubMed:21085179}; OrderedLocusNames=y3579, YPO0599;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP FUNCTION, STRAIN SPECIFICITY, AND DOMAIN.
RC STRAIN=CO-92 / Biovar Orientalis;
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).
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.
CC {ECO:0000269|PubMed:21085179}.
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 CdiI.
CC {ECO:0000305|PubMed:21085179}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Target cell, target cell cytoplasm
CC {ECO:0000305}. Note=Secreted to the cell surface by CdiB, its two
CC partner secretion pathway (TPS) partner (Probable). {ECO:0000305}.
CC -!- DOMAIN: The CDI activity resides in the approximately 220 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-CO92 neutralizes CdiA-CT from strain
CC CO92 but not CdiA-CT from E.coli strains 536 / UPEC, EC93 or from
CC D.dadantii strain 3937). {ECO:0000269|PubMed:21085179}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CdiA toxin
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009952; AAM87127.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL19279.1; -; Genomic_DNA.
DR PIR; AE0074; AE0074.
DR RefSeq; WP_002214945.1; NZ_UAVH01000008.1.
DR RefSeq; YP_002345671.1; NC_003143.1.
DR SMR; Q7CGD9; -.
DR IntAct; Q7CGD9; 3.
DR STRING; 214092.YPO0599; -.
DR PaxDb; Q7CGD9; -.
DR EnsemblBacteria; AAM87127; AAM87127; y3579.
DR GeneID; 57974018; -.
DR KEGG; ype:YPO0599; -.
DR KEGG; ypk:y3579; -.
DR PATRIC; fig|214092.21.peg.855; -.
DR eggNOG; COG3210; Bacteria.
DR HOGENOM; CLU_000043_2_1_6; -.
DR OMA; EFYEYQY; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR010069; CdiA_FHA1_rpt.
DR InterPro; IPR024973; ESPR.
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; PF13018; ESPR; 1.
DR Pfam; PF13332; Fil_haemagg_2; 3.
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; 14.
PE 3: Inferred from homology;
KW Membrane; Reference proteome; Target cell cytoplasm; Toxin; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..3295
FT /note="Toxin CdiA"
FT /id="PRO_0000432091"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 33..366
FT /note="Two-partner system transport domain (TPS)"
FT /evidence="ECO:0000250|UniProtKB:Q3YL96"
FT REGION 353..1574
FT /note="FHA-1"
FT /evidence="ECO:0000305"
FT REGION 1165..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1575..1796
FT /note="Receptor binding domain (RBD)"
FT /evidence="ECO:0000250|UniProtKB:A0A1S4NYE3"
FT REGION 1797..1977
FT /note="YP domain"
FT /evidence="ECO:0000250|UniProtKB:Q3YL96"
FT REGION 1806..1831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1998..2035
FT /note="Periplasmic FHA-1 repeat (pFR)"
FT /evidence="ECO:0000305"
FT REGION 2022..2676
FT /note="FHA-2"
FT /evidence="ECO:0000305"
FT REGION 2260..2292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2823..2847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3073..3295
FT /note="CT domain"
FT /evidence="ECO:0000305|PubMed:21085179"
FT REGION 3276..3295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3073..3076
FT /note="VENN CT cleavage motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 2275..2292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2823..2837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3295 AA; 338791 MW; 312FD349EF696D60 CRC64;
MNKNLYRIVF NQARGMLMVV ADIAASGRAA SSPSSGVGHT QRRRVSALSP LSFRLLIALG
CISLSAQAAI VADGSAPGNQ QPTIISSANG TPQVNIQTPS SGGVSRNAYR QFDVDNRGVI
LNNGRGVNQT QIAGLVDGNP WLARGEASVI LNEVNSRDPS QLNGYIEVAG RKAQVVIANP
AGITCEGCGF INANRATLTT GQAQLNNGQL TGYDVERGEI VIQGKGLDSR GQDHTDLIAR
SVKVNAGIWA NELNITTGRN QVDAAHQNIN TNAADGRHRP AVAVDVANLG GMYAGKIRLI
GTETGVGVHN AGEIGASAGD IVITADGMLV NRGQISSAQQ LAVNTPSGIE NSGVLYGKGN
TQLTTAGKLS NSGTVAAAGD TLIRAAEVNS SRNSVLGAGI KSDNSAITRG TLDIKARGQL
TAQGKNISGT AQTFNANRID LSGSQTQSGD LTFTTEGGDI DLTGANLFAN RRLSVSTPSL
LRTDKANLFA EQIALDAQAL ANVGGVITQT GLTDFNLNLP GDIDNRDGTL LTRGNFLLQA
EHLTSNSQSL LGAGIQSDGK LAPRGDLNVT TRHALIAQGK TLTAGTLALS GSRLDLTDSL
TQAKYMRLTA TEGDIALTGA TVMAANTLFA DTRQILRSDK AYLTADQINL TAYSLSNVEG
RVVQKGSGDF RLDLPGYLDN RGGVLLTKGN LALQAERLTS NSQSLLGAGI QADGSKASKG
DLQANTTQAL IAQGQNVAAG TMTLSGSRVD LTGSQTHASN ITITARDGDV TTREATLITP
GTLSMTAVAN PEQTLNNRGG KLHADNIQLN LAKLENSNGE IAAATDLWLR LQSDFIHQAG
ARLTAGRDLL FNSRGALINQ YKLEAGRDMQ LTALSIRNTS ADRNTNADNS SLLAGRGLSL
STDSLFNRGA IYTTGVGQFT VNGNTENIGE IYTEQQLTFT ATGNLANRGV MQTRGEMQLS
AQGDVNNSGM LYSAGDQMRL SIAGNLTNEG KLHVANGEMR LLTEGNLDNR GSLYGAGNSD
ITTQGNAVNT GSVYTQGALQ WLTKGSVRNS ASIAALGDLQ LRANDLLSDN QSLMAAGLKA
DGSRSDSGNL AVSTEQALIA QGQNIAAGSL ALAGSQIDLT GSQTQANAIS LTAKSGDITL
TSAVIKAATQ LLVTQLAATR SSFIPPSSIP PSSTQSSSTQ ASASPSAWLR TDKASLIADQ
LTFDVQALSN LGGVIAQTGA TDFNLNLPGY LDNRGGTILS KGNVAIQAQG LDSDSGSLLG
AGVQSDGKLT NAGDLAVTVR QDLIAHGQSL AAGAMTLTGS GVDLTGSQTQ ARGITITANK
GDVSTQRANI LSLGSLAINA GANAGQTLNN QGGSLQANNI ALNLGQLDNR TGKIAASQDL
VLGLQSDFNI LADSTLQAGR DFSFTTHGAL TNDGQLLAGR KLSTRSNSLL NNGNIRAVQA
DLRASGALTN RGEILTRGGL STDANTLFNS GTLIGATATL NARERITNSG PNALIGATDK
NGTLALLAPV IENSDTVTRT DTAPTTTLLG MGKVILAGGQ DNSGNYSSAA QVLNLSGLIE
SGNDLLVYAK TLTNRRQILT ATTDFIVGDT ETGAAYWTAE NPDIPGGRYT QPPAGGPMNS
DYIGTNYTST VAYNRIDQIS PEAQLLAGGN LTLQVGTLEN NWSKVSAQGV IDLTGVTLQQ
DDWGSQQRLV EQTTSSGEYR YRTYKGKLWG IAWGPEMKLR LNNQYASSIT AKTLTGSGTV
INNTVINNGA APGAIVAPRD RDSTGKNIAV EFNGIALTLP RSGLYQLKTD KGDYAPGPEA
ALSLANISPP SSLDATGPRG VPPPSDDLNR TGLVTPDRAV SGGYLVETHP AFASLNNWKG
SDLYLQQLSS DPSVIHKRLG DNAYEQRLLR DQVLALTGRT VASDYRSEQA QFEQLFAAGV
QYSKAFNLAP GTRLSAEQMA TLTGNIVLME NRDVAGQTVL VPVVYLAGVK PGDLRANGAL
IAAENISLTE VQGFANAGAI SASNNLQISM AKDITLNNRC GLLQAGNHLQ LSTLNSDIDL
TSARLNATNL QLDSGRDVIL RTASDQYSSG NGAVQRTQTI LGPLASLNIS NNAVITAQRD
FIQQGAGINI GKDLQVNTGG DWLLSTVQRS DQISAQYGGG SATSGSLRHL GSEVKVGGAL
SANVDNLTAV GARVNAGTID VRAQNITLSA ATDSLSVTGG SSSKRHTSSV NLYDETLLGS
QLNATGDINL QTVNDITLSA SAVQTDGALK LAAGGDVTLT SQTEQHDEQR NHTGTKKGLL
SSTTTRSEEG RSQTLAVGSM LSAGSIDVSS QNIAVAGSSV VADKDIRLRA QENLTVSTAQ
QSESGSQLFE QKKSGLMSTG GIGVFIGTSR QKTTDQTQTV SHVGSTVGSL TGNVRLEAGN
QLTLHGSDVV AGKDLALTGA DVAISAAENS RSQQYTAESK QRGLTVALSG PVGSAVNTAV
TTAKAAREEN TGRLAGLQGV KAALSGVQAV QAGQLVQAQG GGITEMVGVS VSLGSQKSSS
QQQQEQTQVS GSALTAGNNL SIKASGSDIL IAGSQLKAGG DTRLDAARDV QLLGAANRQK
TDGSNSSRGG SVGVSVGGSG LSVFANANKG QGNERGDGTF WTETTVDSGG MFSLRSGRDT
ALTGAQVSAE TVKADVGRNL TLQSQQDRDN YDAKQSRASG GISVPVAGGG AAVNLSMSRD
RLSSQYDSVQ AQTGIFAGSG GVDIRVGEHT QLDGAVIAST AAADKNTLDT GTLGFSDIKN
KAVFTVEHQG GSLSTGGPVG SDLLSNLGGM VLAGLGNGGY AEGTTQAAVS EGTITVRDTE
NQQQNVDDLS RDTGNANGSI GPIFDKEKEQ NRLKEVQLIG EIGGQALDIA STQGKIIATH
AANDKMKAVK PEDIAAAEKQ WEKAHPGKAA TAEDINQQIY QTAYNQAFNE SGFGTGGPVQ
RGMQAATAAV QGLAGGNMGA ALTGASAPYL AGVIKQSTGD NPAANTMAHA VLGAVTAYAS
GNNALAGAAG AATAELMAPT IISALGWDKN TLTEGQKQAV SALSTLAAGL AGGLTGDSTA
DALAGGQAGK NAVENNLLGG NEFTHTQFVQ KHGADVLSCA DNPSNAACQR GIAENKAYIA
ALATGSVALL PGSSQAMWAL GAGTNAGMQY ADNGKINPVN SVAAGWINVI TMGQGWKGTI
AWNAAGGALI NAINGGDPLT GAITNGTGAG FGYGVGNYVV KPAANTLGKW ITGGWNPKFD
PNLLKYAEVK GQLGISKEML PSKIPSAVGN AGGSLSSEFG SSLIQQKKDA MEDSK
