CEA6_ECOLX
ID CEA6_ECOLX Reviewed; 551 AA.
AC P17999;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Colicin-E6;
DE EC=3.1.-.-;
DE AltName: Full=Ribonuclease;
OS Escherichia coli.
OG Plasmid ColE6-CT14.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2687234; DOI=10.1128/jb.171.12.6430-6436.1989;
RA Akutsu A., Masaki H., Ohta T.;
RT "Molecular structure and immunity specificity of colicin E6, an
RT evolutionary intermediate between E-group colicins and cloacin DF13.";
RL J. Bacteriol. 171:6430-6436(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-551.
RX PubMed=2549375; DOI=10.1007/bf02464892;
RA Lau P.C.K., Condie J.A.;
RT "Nucleotide sequences from the colicin E5, E6 and E9 operons: presence of a
RT degenerate transposon-like structure in the ColE9-J plasmid.";
RL Mol. Gen. Genet. 217:269-277(1989).
CC -!- FUNCTION: Inactivates ribosomes by hydrolyzing 16S RNA in 30S ribosomes
CC at a specific site.
CC -!- FUNCTION: Colicins are polypeptide toxins produced by and active
CC against E.coli and closely related bacteria.
CC -!- SIMILARITY: Belongs to the cloacin colicin family. {ECO:0000305}.
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DR EMBL; X15856; CAA33855.1; -; Genomic_DNA.
DR EMBL; M31808; AAA23080.1; -; Genomic_DNA.
DR PIR; PQ0030; PQ0030.
DR AlphaFoldDB; P17999; -.
DR SMR; P17999; -.
DR GO; GO:0005727; C:extrachromosomal circular DNA; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR Gene3D; 3.10.380.10; -; 1.
DR InterPro; IPR024575; Cloacin_colicin_fam.
DR InterPro; IPR036725; ColE3_ribonuclease_sf.
DR InterPro; IPR009105; Colicin_E3_ribonuclease.
DR InterPro; IPR024566; Colicin_R_dom.
DR InterPro; IPR016128; Pyosin/cloacin_T_dom.
DR InterPro; IPR036302; Pyosin/cloacin_T_dom_sf.
DR Pfam; PF03515; Cloacin; 1.
DR Pfam; PF09000; Cytotoxic; 1.
DR Pfam; PF11570; E2R135; 1.
DR PRINTS; PR01295; CLOACIN.
DR SUPFAM; SSF63840; SSF63840; 1.
DR SUPFAM; SSF69369; SSF69369; 1.
PE 3: Inferred from homology;
KW Antibiotic; Antimicrobial; Bacteriocin; Endonuclease; Hydrolase; Nuclease;
KW Plasmid.
FT CHAIN 1..551
FT /note="Colicin-E6"
FT /id="PRO_0000218678"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..551
FT /note="Ribosome inactivating activity"
FT REGION 517..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..551
FT /note="Binding of immunity protein"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 58011 MW; D223D7F0770392E0 CRC64;
MSGGDGRGHN TGAHSTSGNI NGGPTGLGVG GGASDGSGWS SENNPWGGGS GSGIHWGGGS
GHGNGGGNGN SGGGSGTGGN LSAVAAPVAF GFPALSTPGA GGLAVSISAG ALSAAIADIM
AALKGPFKFG LWGVALYGVL PSQIAKDDPN MMSKIVTSLP ADDITESPVS SLPLDKATVN
VNVRVVDDVK DERQNISVVS GVPMSVPVVD AKPTERPGVF TASIPGAPVL NISVNNSTPA
VQTLSPGVTN NTDKDVRPAG FTQGGNTRDA VIRFPKDSGH NAVYVSVSDV LSPDQVKQRQ
DEENRRQQEW DATHPVEAAE RNYERARAEL NQANEDVARN QERQAKAVQV YNSRKSELDA
ANKTLADAIA EIKQFNRFAH DPMAGGHRMW QMAGLKAQRA QTDVNNKQAA FDAAAKEKSD
ADAALSSAME SRKKKEDKKR SAENKLNEEK NKPRKGVKDY GHDYHPDPKT EDIKGLGELK
EGKPKTPKQG GGGKRARWYG DKGRKIYEWD SQHGELEGYR ASDGQHLGSF EPKTGNQLKG
PDPKRNIKKY L