ID   CEAC_ECOLX              Reviewed;         561 AA.
AC   P00645;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Cloacin;
DE            EC=3.1.-.-;
DE   AltName: Full=Ribonuclease;
GN   Name=ccl;
OS   Escherichia coli.
OG   Plasmid Clo DF13.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3749334; DOI=10.1016/0147-619x(86)90072-7;
RA   Nijkamp H.J.J., de Lang R., Stuitje A.R., van den Elsen P.J.M.,
RA   Veltkamp E., van Putten A.J.;
RT   "The complete nucleotide sequence of the bacteriocinogenic plasmid
RT   CloDF13.";
RL   Plasmid 16:135-160(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6344017; DOI=10.1093/nar/11.8.2465;
RA   van den Elzen P.J.M., Walters H.H.B., Veltkamp E., Nijkamp H.J.J.;
RT   "Molecular structure and function of the bacteriocin gene and bacteriocin
RT   protein of plasmid Clo DF13.";
RL   Nucleic Acids Res. 11:2465-2477(1983).
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   -!- MISCELLANEOUS: Plasmid Clo DF13 originates from E.cloacae but is stably
CC       maintained in and studied mostly from E.coli.
CC   -!- SIMILARITY: Belongs to the cloacin colicin family. {ECO:0000305}.
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DR   EMBL; X04466; CAA28147.1; -; Genomic_DNA.
DR   PIR; A00791; CDECP3.
DR   RefSeq; NP_052372.1; NC_002119.1.
DR   RefSeq; WP_010891190.1; NC_002119.1.
DR   AlphaFoldDB; P00645; -.
DR   SMR; P00645; -.
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..561
FT                   /note="Cloacin"
FT                   /id="PRO_0000218679"
FT   REGION          1..180
FT                   /note="Involved in the translocation of the protein across
FT                   the cell membrane"
FT                   /evidence="ECO:0000305"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..420
FT                   /note="Responsible for the receptor binding activity"
FT   REGION          254..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..561
FT                   /note="Ribonuclease activity"
FT   REGION          432..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..561
FT                   /note="Binding of immunity protein"
FT   COMPBIAS        15..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        112
FT                   /note="P -> L (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   561 AA;  59278 MW;  E4B21DB5DEEDFF74 CRC64;
     MSGGDGRGPG NSGLGHNGGQ ASGNVNGTSG KGGPSSGGGT DPNSGPGWGT THTPNGDIHN
     YNPGEFGNGG SKPGGNGGNS GNHSGSSGGG QSSATAMAFG LPALATPGAE GPALSFSGDA
     LSSAVADVLA ALKGPFKFGL WGIAIYGVLP SEIAKDDPKM MSKIMTSLPA DTVTETPAST
     LPLDQATVRV RQRVVDVVKD ERQHIAVVAG RPMSVPVVDA KPTKRPGVFS VSIPGLPALQ
     VSVPKGVPAA KAPPKGIVAE KGDSRPAGFT AGGNSREAVI RFPKETGQKP VYVSVTDVLT
     PAQVKQRQEE EKRRQQAWDA AHPEEGLKRE YDKAKAELDA EDKNITTLNG RITSTEKAIP
     GARAAVQEAD KKVKEAEANK DDFVTYNPPH EYGSGWQDQV RYLDKDIQNQ NAKLKAAQAS
     LNAMNDALSR DKAALSGAME SRKQKEKKAK EAENKLNEEK KKPRKGTKDY GHDYFPDPKT
     EDIKGLGELK EGKPKTPKQG GGGKRARWYG DKKRKIYEWD SQHGELEGYR ASDGEHLGAF
     DPKTGKQVKG PDPKRNIKKY L