ID CEA9_ECOLX Reviewed; 582 AA. AC P09883; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 4. DT 02-SEP-2026, entry version 138. DE RecName: Full=Colicin-E9; DE EC=3.1.-.-; GN Name=col; Synonyms=cei; OS Escherichia coli. OG Plasmid ColE9. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA James R.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 378-582. 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). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 509-582. RX PubMed=2646600; DOI=10.1093/nar/17.4.1761; RA Eaton T., James R.; RT "Complete nucleotide sequence of the colicin E9 (cei) gene."; RL Nucleic Acids Res. 17:1761-1761(1989). CC -!- FUNCTION: This plasmid-coded bactericidal protein is an endonuclease CC active on both single- and double-stranded DNA but with undefined CC specificity. CC -!- FUNCTION: Colicins are polypeptide toxins produced by and active CC against E.coli and closely related bacteria. CC -!- INTERACTION: CC P09883; P04482: imm; NbExp=4; IntAct=EBI-1029888, EBI-15855054; CC P09883; P13479: imm; NbExp=4; IntAct=EBI-1029888, EBI-1029882; CC P09883; P02931: ompF; Xeno; NbExp=4; IntAct=EBI-1029888, EBI-371336; CC P09883; P0A855: tolB; Xeno; NbExp=9; IntAct=EBI-1029888, EBI-7180728; CC -!- SIMILARITY: Belongs to the colicin/pyosin nuclease family. CC {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; X12591; CAA31104.1; -; Genomic_DNA. DR EMBL; X15858; CAA33862.1; -; Genomic_DNA. DR PIR; PQ0032; PQ0032. DR RefSeq; WP_012644886.1; NC_011977.1. DR PDB; 1BXI; X-ray; 2.05 A; B=449-582. DR PDB; 1EMV; X-ray; 1.70 A; B=450-582. DR PDB; 1FR2; X-ray; 1.60 A; B=450-582. DR PDB; 1FSJ; X-ray; 1.80 A; B/C/D/E=450-582. DR PDB; 1V13; X-ray; 2.00 A; A/B=450-582. DR PDB; 1V14; X-ray; 2.90 A; A/B/C/D=450-582. DR PDB; 1V15; X-ray; 2.40 A; A/B/C/D=450-582. DR PDB; 2GYK; X-ray; 1.60 A; B/F=450-582. DR PDB; 2GZE; X-ray; 1.80 A; B=450-582. DR PDB; 2GZF; X-ray; 1.75 A; B=450-582. DR PDB; 2GZG; X-ray; 1.70 A; B=450-582. DR PDB; 2GZI; X-ray; 1.70 A; B=450-582. DR PDB; 2GZJ; X-ray; 1.60 A; B/F=450-582. DR PDB; 2IVZ; X-ray; 2.00 A; E/F/G/H=32-47. DR PDB; 2K5X; NMR; -; B=450-582. DR PDB; 2VLN; X-ray; 1.60 A; B=450-582. DR PDB; 2VLO; X-ray; 1.80 A; B=450-582. DR PDB; 2VLP; X-ray; 2.00 A; B=450-582. DR PDB; 2VLQ; X-ray; 1.60 A; B=450-582. DR PDB; 2WPT; X-ray; 1.78 A; B=450-582. DR PDB; 3O0E; X-ray; 3.01 A; L/M/N/O/P/Q=2-18. DR PDB; 4JML; X-ray; 2.00 A; E=32-47. DR PDB; 5EW5; X-ray; 3.20 A; A/B/C/D=1-582. DR PDB; 7NST; EM; 3.70 A; D=1-314. DR PDB; 7NSU; EM; 4.70 A; D=1-582. DR AlphaFoldDB; P09883; -. DR BMRB; P09883; -. DR EMDB; EMD-12576; -. DR EMDB; EMD-12577; -. DR EMDB; EMD-2372; -. DR MDposit; P09883; -. DR MDRepo; P09883; -. DR SMR; P09883; -. DR DIP; DIP-16992N; -. DR IntAct; P09883; 6. DR MINT; P09883; -. DR TCDB; 1.C.1.4.1; the channel-forming colicin (colicin) family. DR EvolutionaryTrace; P09883; -. DR GO; GO:0005727; C:extrachromosomal circular DNA; IEA:InterPro. DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA. DR GO; GO:0004519; F:endonuclease activity; IDA:CAFA. DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA. DR DisProt; DP00342; -. DR FunFam; 3.90.540.10:FF:000001; Colicin-E9; 1. DR Gene3D; 3.90.540.10; Colicin/pyocin, DNase domain; 1. DR Gene3D; 1.10.287.620; Helix Hairpins; 1. DR Gene3D; 1.20.5.740; Single helix bin; 1. DR InterPro; IPR024575; Cloacin_colicin. DR InterPro; IPR037146; Colicin/pyocin_DNase_dom_sf. DR InterPro; IPR024566; Colicin_R_dom. DR InterPro; IPR044925; His-Me_finger_sf. DR InterPro; IPR016128; Pyosin/cloacin_T_dom. DR InterPro; IPR036302; Pyosin/cloacin_T_dom_sf. DR Pfam; PF03515; Cloacin; 1. DR Pfam; PF21431; Col-Pyo_DNase; 1. DR Pfam; PF11570; E2R135; 1. DR PRINTS; PR01295; CLOACIN. DR SUPFAM; SSF69369; Cloacin translocation domain; 1. DR SUPFAM; SSF69985; Colicin E3 receptor domain; 1. DR SUPFAM; SSF54060; His-Me finger endonucleases; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin; Endonuclease; KW Hydrolase; Metal-binding; Nuclease; Plasmid; Zinc. FT CHAIN 1..582 FT /note="Colicin-E9" FT /id="PRO_0000218684" FT REGION 1..74 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 246..270 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 294..321 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 422..489 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 510..542 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..35 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..45 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 46..74 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 297..321 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 430..453 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 465..476 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 516..529 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 550 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 575 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 579 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT CONFLICT 511 FT /note="K -> R (in Ref. 3)" FT /evidence="ECO:0000305" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:2IVZ" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 114..124 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 142..148 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 155..161 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 178..191 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 194..211 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 221..224 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 230..233 FT /evidence="ECO:0007829|PDB:5EW5" FT TURN 262..267 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 268..274 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 281..283 FT /evidence="ECO:0007829|PDB:5EW5" FT STRAND 284..290 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 294..313 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 316..375 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 376..381 FT /evidence="ECO:0007829|PDB:5EW5" FT HELIX 452..454 FT /evidence="ECO:0007829|PDB:1FR2" FT STRAND 457..460 FT /evidence="ECO:0007829|PDB:1V13" FT HELIX 470..473 FT /evidence="ECO:0007829|PDB:1FR2" FT STRAND 476..478 FT /evidence="ECO:0007829|PDB:2WPT" FT HELIX 484..490 FT /evidence="ECO:0007829|PDB:1FR2" FT STRAND 494..497 FT /evidence="ECO:0007829|PDB:1FR2" FT HELIX 498..511 FT /evidence="ECO:0007829|PDB:1FR2" FT HELIX 513..516 FT /evidence="ECO:0007829|PDB:1FR2" FT STRAND 517..519 FT /evidence="ECO:0007829|PDB:1BXI" FT HELIX 521..528 FT /evidence="ECO:0007829|PDB:1FR2" FT HELIX 531..533 FT /evidence="ECO:0007829|PDB:1FR2" FT HELIX 537..539 FT /evidence="ECO:0007829|PDB:1FR2" FT STRAND 548..553 FT /evidence="ECO:0007829|PDB:1FR2" FT HELIX 555..557 FT /evidence="ECO:0007829|PDB:1FR2" FT STRAND 561..563 FT /evidence="ECO:0007829|PDB:1FR2" FT HELIX 564..566 FT /evidence="ECO:0007829|PDB:1FR2" FT STRAND 567..570 FT /evidence="ECO:0007829|PDB:1FR2" FT HELIX 572..579 FT /evidence="ECO:0007829|PDB:1FR2" SQ SEQUENCE 582 AA; 61587 MW; 47A71B57B45AFDD9 CRC64; MSGGDGRGHN TGAHSTSGNI NGGPTGIGVS GGASDGSGWS SENNPWGGGS GSGIHWGGGS GRGNGGGNGN SGGGSGTGGN LSAVAAPVAF GFPALSTPGA GGLAVSISAS ELSAAIAGII AKLKKVNLKF TPFGVVLSSL IPSEIAKDDP NMMSKIVTSL PADDITESPV SSLPLDKATV NVNVRVVDDV KDERQNISVV SGVPMSVPVV DAKPTERPGV FTASIPGAPV LNISVNDSTP AVQTLSPGVT NNTDKDVRPA GFTQGGNTRD AVIRFPKDSG HNAVYVSVSD VLSPDQVKQR QDEENRRQQE WDATHPVEAA ERNYERARAE LNQANEDVAR NQERQAKAVQ VYNSRKSELD AANKTLADAI AEIKQFNRFA HDPMAGGHRM WQMAGLKAQR AQTDVNNKQA AFDAAAKEKS DADAALSAAQ ERRKQKENKE KDAKDKLDKE SKRNKPGKAT GKGKPVGDKW LDDAGKDSGA PIPDRIADKL RDKEFKSFDD FRKAVWEEVS KDPELSKNLN PSNKSSVSKG YSPFTPKNQQ VGGRKVYELH HDKPISQGGE VYDMDNIRVT TPKRHIDIHR GK //