CEA3_ECOLX
ID CEA3_ECOLX Reviewed; 551 AA.
AC P00646;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Colicin-E3;
DE EC=3.1.-.-;
DE AltName: Full=Colicin-E3 A chain;
DE AltName: Full=Ribonuclease;
GN Name=ceaC;
OS Escherichia coli.
OG Plasmid ColE3-CA38.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3889348; DOI=10.1016/0022-2836(85)90340-7;
RA Masaki H., Ohta T.;
RT "Colicin E3 and its immunity genes.";
RL J. Mol. Biol. 182:217-227(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 370-551.
RX PubMed=6095211; DOI=10.1093/nar/12.22.8733;
RA Lau P.C.K., Rowsome R.W., Zuker M., Visentin L.P.;
RT "Comparative nucleotide sequences encoding the immunity proteins and the
RT carboxyl-terminal peptides of colicins E2 and E3.";
RL Nucleic Acids Res. 12:8733-8745(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 428-551.
RX PubMed=6344012; DOI=10.1093/nar/11.11.3547;
RA Mock M., Miyada C.G., Gunsalus R.P.;
RT "Nucleotide sequence for the catalytic domain of colicin E3 and its
RT immunity protein. Evidence for a third gene overlapping colicin.";
RL Nucleic Acids Res. 11:3547-3557(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 445-551.
RX PubMed=6295812; DOI=10.1016/0014-5793(82)81087-9;
RA Masaki H., Ohta T.;
RT "A plasmid region encoding the active fragment and the inhibitor protein of
RT colicin E3-CA38.";
RL FEBS Lett. 149:129-132(1982).
RN [5]
RP PROTEIN SEQUENCE OF 455-551.
RX PubMed=730747; DOI=10.1093/oxfordjournals.jbchem.a132217;
RA Suzuki K., Imahori K.;
RT "Amino acid sequence of an active fragment (T2A) of colicin E3.";
RL J. Biochem. 84:1031-1039(1978).
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 -!- INTERACTION:
CC P00646; P02984: imm; NbExp=2; IntAct=EBI-1029919, EBI-1029912;
CC -!- SIMILARITY: Belongs to the cloacin colicin family. {ECO:0000305}.
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DR EMBL; J01574; AAA88416.1; -; Genomic_DNA.
DR EMBL; X02397; CAA26241.1; -; Genomic_DNA.
DR EMBL; X01162; CAA25607.1; -; Genomic_DNA.
DR PIR; S07269; NRECE3.
DR RefSeq; WP_000012964.1; NZ_RRTR01000103.1.
DR PDB; 1E44; X-ray; 2.40 A; B=456-551.
DR PDB; 1JCH; X-ray; 3.02 A; A/C=1-551.
DR PDB; 1UJW; X-ray; 2.75 A; B=314-448.
DR PDB; 2B5U; X-ray; 2.30 A; A/C=1-551.
DR PDB; 4UDM; X-ray; 2.96 A; B=456-551.
DR PDB; 4V5K; X-ray; 3.20 A; AY/CY=455-551.
DR PDBsum; 1E44; -.
DR PDBsum; 1JCH; -.
DR PDBsum; 1UJW; -.
DR PDBsum; 2B5U; -.
DR PDBsum; 4UDM; -.
DR PDBsum; 4V5K; -.
DR AlphaFoldDB; P00646; -.
DR SMR; P00646; -.
DR DIP; DIP-545N; -.
DR IntAct; P00646; 2.
DR DrugBank; DB04039; 3-Oxo-Pentadecanoic Acid.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR PRIDE; P00646; -.
DR EvolutionaryTrace; P00646; -.
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:0044325; F:transmembrane transporter binding; IPI:CAFA.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0032413; P:negative regulation of ion transmembrane transporter activity; IDA:CAFA.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; Endonuclease; Hydrolase; Nuclease; Plasmid.
FT CHAIN 1..551
FT /note="Colicin-E3"
FT /id="PRO_0000218677"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..505
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 COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1JCH"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1JCH"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1JCH"
FT TURN 261..266
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 293..313
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 315..375
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:1JCH"
FT HELIX 386..448
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:2B5U"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:1JCH"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:2B5U"
FT TURN 501..504
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 505..510
FT /evidence="ECO:0007829|PDB:2B5U"
FT TURN 511..514
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:2B5U"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:2B5U"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:2B5U"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:2B5U"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:2B5U"
SQ SEQUENCE 551 AA; 57963 MW; E444CE918D89ECD6 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 SAENNLNDEK NKPRKGFKDY GHDYHPAPKT ENIKGLGDLK
PGIPKTPKQN GGGKRKRWTG DKGRKIYEWD SQHGELEGYR ASDGQHLGSF DPKTGNQLKG
PDPKRNIKKY L
