ID CEAM_ECOLX Reviewed; 271 AA.
AC P05820;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 28-JUN-2023, entry version 99.
DE RecName: Full=Colicin-M;
GN Name=cma;
OS Escherichia coli.
OG Plasmid ColBM-Cl139.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036784; DOI=10.1128/jb.169.7.3358-3361.1987;
RA Koeck J., Oelschlaeger T., Kamp R.M., Braun V.;
RT "Primary structure of colicin M, an inhibitor of murein biosynthesis.";
RL J. Bacteriol. 169:3358-3361(1987).
CC -!- FUNCTION: Colicins are polypeptide toxins produced by and active
CC against E.coli and closely related bacteria.
CC -!- FUNCTION: This is a calcium-requiring inhibitor for murein
CC biosynthesis; it causes lysis of sensitive cells accompanied by murein
CC degradation. The target site is possibly the cytoplasmic membrane.
CC -!- MISCELLANEOUS: This colicin requires TonB for its uptake.
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DR EMBL; M16754; AAA23589.1; -; Genomic_DNA.
DR PIR; A27090; IKECM.
DR RefSeq; WP_000449473.1; NZ_WXYX01000005.1.
DR RefSeq; YP_008998009.1; NC_023315.1.
DR PDB; 2XMX; X-ray; 1.67 A; A/B=1-271.
DR PDB; 2XTQ; X-ray; 2.31 A; A/B/C/D/E/F/G/H=1-271.
DR PDB; 2XTR; X-ray; 2.14 A; A/B=1-271.
DR PDB; 3DA3; X-ray; 2.50 A; A/B=1-271.
DR PDB; 3DA4; X-ray; 1.70 A; A/B=1-271.
DR PDBsum; 2XMX; -.
DR PDBsum; 2XTQ; -.
DR PDBsum; 2XTR; -.
DR PDBsum; 3DA3; -.
DR PDBsum; 3DA4; -.
DR AlphaFoldDB; P05820; -.
DR SMR; P05820; -.
DR IntAct; P05820; 1.
DR EvolutionaryTrace; P05820; -.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1440.280; -; 1.
DR Gene3D; 3.30.450.400; Colicin M, catalytic domain; 1.
DR InterPro; IPR028056; Colicin_M.
DR Pfam; PF14859; Colicin_M; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin; Plasmid; TonB box.
FT CHAIN 1..271
FT /note="Colicin-M"
FT /id="PRO_0000218689"
FT MOTIF 2..9
FT /note="TonB box"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 49..65
FT /evidence="ECO:0007829|PDB:2XMX"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2XTQ"
FT HELIX 70..92
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2XMX"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3DA4"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:2XMX"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3DA4"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:2XMX"
FT STRAND 173..184
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:2XMX"
FT STRAND 198..209
FT /evidence="ECO:0007829|PDB:2XMX"
FT STRAND 213..231
FT /evidence="ECO:0007829|PDB:2XMX"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:2XMX"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:2XMX"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:2XMX"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:2XMX"
SQ SEQUENCE 271 AA; 29483 MW; B41B7BE107EC1DBA CRC64;
METLTVHAPS PSTNLPSYGN GAFSLSAPHV PGAGPLLVQV VYSFFQSPNM CLQALTQLED
YIKKHGASNP LTLQIISTNI GYFCNADRNL VLHPGISVYD AYHFAKPAPS QYDYRSMNMK
QMSGNVTTPI VALAHYLWGN GAERSVNIAN IGLKISPMKI NQIKDIIKSG VVGTFPVSTK
FTHATGDYNV ITGAYLGNIT LKTEGTLTIS ANGSWTYNGV VRSYDDKYDF NASTHRGIIG
ESLTRLGAMF SGKEYQILLP GEIHIKESGK R
//
