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RHSB_DICD3
ID   RHSB_DICD3              Reviewed;        1436 AA.
AC   E0SIS2;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Probable deoxyribonuclease RhsB;
DE            EC=3.1.-.-;
DE   AltName: Full=DNase RhsB;
DE   AltName: Full=Toxin RhsB;
GN   Name=rhsB; OrderedLocusNames=Dda3937_02773;
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   PROBABLE FUNCTION AS A DNASE, FUNCTION AS A TOXIN, EXPRESSION IN E.COLI,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=3937;
RX   PubMed=23572593; DOI=10.1073/pnas.1300627110;
RA   Koskiniemi S., Lamoureux J.G., Nikolakakis K.C., t'Kint de Roodenbeke C.,
RA   Kaplan M.D., Low D.A., Hayes C.S.;
RT   "Rhs proteins from diverse bacteria mediate intercellular competition.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:7032-7037(2013).
CC   -!- FUNCTION: Toxic component of a toxin-immunity protein module, which
CC       functions as a cellular contact-dependent growth inhibition (CDI)
CC       system. This protein may be a nuclease that is specifically inhibited
CC       by its cognate immunity protein RhsBI. Upon expression of the C-
CC       terminus (residues 1284-1436) in E.coli growth is inhibited, cells
CC       elongate, nucleoids condense and plasmid DNA is degraded; these effects
CC       are blocked specifically by cognate immunity protein RshIB. Cell
CC       contact is necessary for growth inhibition.
CC       {ECO:0000269|PubMed:23572593}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: A double rhsB-rhsIB deletion is outcompeted by
CC       wild-type cells, restoration of rhsIB restores normal growth in
CC       competition experiments. Restoration of growth requires the RhsB-
CC       specific immunity protein, rhsIA does not restore growth.
CC       {ECO:0000269|PubMed:23572593}.
CC   -!- SIMILARITY: Belongs to the RHS/WapA nuclease family. {ECO:0000305}.
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DR   EMBL; CP002038; ADM99131.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0SIS2; -.
DR   SMR; E0SIS2; -.
DR   STRING; 198628.Dda3937_02773; -.
DR   PRIDE; E0SIS2; -.
DR   EnsemblBacteria; ADM99131; ADM99131; Dda3937_02773.
DR   KEGG; ddd:Dda3937_02773; -.
DR   eggNOG; COG3209; Bacteria.
DR   eggNOG; COG4104; Bacteria.
DR   HOGENOM; CLU_001218_1_8_6; -.
DR   OMA; EGRTWRY; -.
DR   Proteomes; UP000006859; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00085; HNHc; 1.
DR   InterPro; IPR045351; DUF6531.
DR   InterPro; IPR003615; HNH_nuc.
DR   InterPro; IPR008727; PAAR_motif.
DR   InterPro; IPR022385; Rhs_assc_core.
DR   InterPro; IPR031325; RHS_repeat.
DR   InterPro; IPR006530; YD.
DR   Pfam; PF20148; DUF6531; 1.
DR   Pfam; PF05488; PAAR_motif; 1.
DR   Pfam; PF05593; RHS_repeat; 6.
DR   TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
DR   TIGRFAMs; TIGR01643; YD_repeat_2x; 8.
PE   1: Evidence at protein level;
KW   Hydrolase; Membrane; Nuclease; Reference proteome; Repeat; Toxin;
KW   Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..1436
FT                   /note="Probable deoxyribonuclease RhsB"
FT                   /id="PRO_0000423973"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          486..521
FT                   /note="YD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          569..605
FT                   /note="YD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          612..647
FT                   /note="YD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          766..799
FT                   /note="YD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          847..879
FT                   /note="YD 5"
FT                   /evidence="ECO:0000255"
FT   REGION          16..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1436 AA;  161673 MW;  72D014EAC5944262 CRC64;
     MLNDILSRVA RVGAMHAGNR PNPPADRPQP CQGKPPTSPG KTIKHKSFLG ALAGAVAGAL
     VAAAVAAAAV FLVGVTGGLA VAAVGALAVF AAGDLISAVT NKVSAVVDSA SPAFGPVASG
     SGNVFVEKQP VARATKDTVA CTKHNSPQLI AQGSESVFVN DAPAARIDDK TVCGATLKEG
     ASTVFFGSGQ GTYLEIADEF SWWEKALLIA VEFLVPPSRG MLKGLGKLFT RNGLKSVLKG
     AKAGALFITK VPGKMGCAAR AFKANKGMAR FKEAAKAFKK DPVYLASGEV IESRTDIELG
     QTLPLVFERT YRSASAHTGL LGRGWHDSWS EVATVTHDGL NTHVVITLAQ GYDIDFTFHQ
     DVQAVYCPHY PEFTLHRRGD GFSLWHRDQQ TWRDFSVVQG ERRLLSAIHD SHDNRIELVR
     DPKGYLRQLR HSDGVTLLLV WQGEYLHQIQ RIDGGQKTLL AEYRQDEQGR LVEANATHAY
     HLYYEYNTAH RLTRWHDNDQ TWARYEYDAQ GRCVYTTCAD GFLTARFDYL PDRVVMTDGL
     GQRSEFGFND LHLMSWEQSP LGHITRYEYD EVGNLLREIS PAGRVVEFTY LDDTGRVSTF
     TDGSGHQWQY DYDDAQRLCG VTDPLGREWG WVYDAEGNPE RLTGPDASEV RFTWNRYGLL
     TQVSDAAGEV QARLQYDHRQ RLLSATDAES RTRQLRYDRQ DRVVQWQRAD GARFRLGYRR
     ASWTLPEQLI RPDDKEEQRQ YDRHNNLLSY VDGNGALWRQ TFGPFDLLTA RTDAEGRTWR
     YEYDRESQQL IAVTAPDGSR WQWWLDADGR VIRERDMTGT ETHYGYDEDG LCIRVRNGEG
     DTRHFLYDAR GLLLRETAPD DTLHYRYDAA GRLTEVSSAT AHVQLDYDLR DRVVREWHNG
     TLLTRQYDDA ARTVTRTLTW DGDADDTTGT LAPLTSLFHY TRTGELRQVQ LPDGADLTLT
     HDAAGRESLR TGGSGFVQQR EYDVMGWLTR EQSGAQHDGR LQPAQTREYR YDGAGNLTGV
     RHNRDAEGYR LDATGRVQEM LSGGAGKPVD TTARFHYTRT GLPQEAGRLT EWQAGRLVQH
     DDTHYQYDRA GRLIRKQVVQ PGYRPQVWQY RWDSRNQLRV VDTPNGERWL YRYDPFGRRV
     GKRCDQKAEE TRYLWDGDQI AEIRHYRHGQ LIQRRHWVYN GWELVVQQRQ HTGGDWETDF
     VTSSQNGTPQ ALFTPDGTLR WQVPKATLWG QRQTEKSESP DPGLAFAGQL RDSESGLCYN
     RFRYYDPAGG CYVSPDPIGI AGGESNYGYV QNPNTRVDPL GLAGCAMGEI LADADKWSLA
     KIGDRQKGMI KDKLSTVKER SKALNTKMRE HFNANEQKII SEWEKQTGMN WPTLSSGSRA
     TPHHVIPIKN GGSNEWWNII PVQHPHTGTI HGTGSALRTH LPYQKDGGKL WNLLGY
 
 
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