ID   LYS0_ECOLX              Reviewed;          49 AA.
AC   P02987;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Lysis protein;
DE   AltName: Full=Bacteriocin release protein;
DE            Short=BRP;
DE   AltName: Full=Protein H;
DE   Flags: Precursor;
GN   Name=H; Synonyms=cex;
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=6163089; DOI=10.1038/290264a0;
RA   Stuitje A.R., Spelt C.E., Veltkamp E., Nijkamp H.J.J.;
RT   "Identification of mutations affecting replication control of plasmid Clo
RT   DF13.";
RL   Nature 290:264-267(1981).
RN   [3]
RP   TRANSLOCATION BY SRP/SEC/YIDC PATHWAY.
RX   PubMed=15140892; DOI=10.1074/jbc.m403229200;
RA   Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.;
RT   "Targeting and translocation of two lipoproteins in Escherichia coli via
RT   the SRP/Sec/YidC pathway.";
RL   J. Biol. Chem. 279:31026-31032(2004).
CC   -!- FUNCTION: Lysis proteins are required for both colicin release and
CC       partial cell lysis.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Targeted by SRP to the Sec
CC       translocon.
CC   -!- MISCELLANEOUS: Plasmid Clo DF13 originates from Enterobacter cloacae
CC       but is stably maintained in and studied mostly from E.coli.
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DR   EMBL; X04466; CAA28145.1; -; Genomic_DNA.
DR   PIR; A03515; ZHECP3.
DR   RefSeq; NP_052370.1; NC_002119.1.
DR   RefSeq; WP_010891188.1; NZ_UNQR01000060.1.
DR   AlphaFoldDB; P02987; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019835; P:cytolysis; IEA:InterPro.
DR   InterPro; IPR003059; Lysis_col.
DR   Pfam; PF02402; Lysis_col; 1.
DR   PRINTS; PR01297; LYSISCOLICIN.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Lipoprotein; Membrane; Palmitate; Plasmid; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..49
FT                   /note="Lysis protein"
FT                   /id="PRO_0000005679"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   49 AA;  5157 MW;  1A3DC979EBB0C5DC CRC64;
     MKKAKAIFLF ILIVSGFLLV ACQANYIRDV QGGTVAPSSS SELTGIAVQ