CEA9_ECOLX
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 03-AUG-2022, entry version 125.
DE RecName: Full=Colicin-E9;
DE EC=3.1.-.-;
GN Name=col; Synonyms=cei;
OS Escherichia coli.
OG Plasmid ColE9.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 RefSeq; YP_002533537.1; 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 PDBsum; 1BXI; -.
DR PDBsum; 1EMV; -.
DR PDBsum; 1FR2; -.
DR PDBsum; 1FSJ; -.
DR PDBsum; 1V13; -.
DR PDBsum; 1V14; -.
DR PDBsum; 1V15; -.
DR PDBsum; 2GYK; -.
DR PDBsum; 2GZE; -.
DR PDBsum; 2GZF; -.
DR PDBsum; 2GZG; -.
DR PDBsum; 2GZI; -.
DR PDBsum; 2GZJ; -.
DR PDBsum; 2IVZ; -.
DR PDBsum; 2K5X; -.
DR PDBsum; 2VLN; -.
DR PDBsum; 2VLO; -.
DR PDBsum; 2VLP; -.
DR PDBsum; 2VLQ; -.
DR PDBsum; 2WPT; -.
DR PDBsum; 3O0E; -.
DR PDBsum; 4JML; -.
DR PDBsum; 5EW5; -.
DR PDBsum; 7NST; -.
DR PDBsum; 7NSU; -.
DR AlphaFoldDB; P09883; -.
DR BMRB; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific 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:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:CAFA.
DR CDD; cd00085; HNHc; 1.
DR DisProt; DP00342; -.
DR Gene3D; 3.90.540.10; -; 1.
DR InterPro; IPR024575; Cloacin_colicin_fam.
DR InterPro; IPR037146; Colicin/pyocin_DNase_dom_sf.
DR InterPro; IPR024566; Colicin_R_dom.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR003615; HNH_nuc.
DR InterPro; IPR016128; Pyosin/cloacin_T_dom.
DR InterPro; IPR036302; Pyosin/cloacin_T_dom_sf.
DR Pfam; PF03515; Cloacin; 1.
DR Pfam; PF11570; E2R135; 1.
DR PRINTS; PR01295; CLOACIN.
DR SUPFAM; SSF54060; SSF54060; 1.
DR SUPFAM; SSF69369; SSF69369; 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 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..539
FT /note="Polar residues"
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 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 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 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
