CEAB_ECOLX
ID CEAB_ECOLX Reviewed; 511 AA.
AC P05819;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Colicin-B;
GN Name=cba;
OS Escherichia coli.
OG Plasmid ColBM-pF166.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2439491; DOI=10.1128/jb.169.7.3350-3357.1987;
RA Schramm E., Mende J., Braun V., Kamp R.M.;
RT "Nucleotide sequence of the colicin B activity gene cba: consensus
RT pentapeptide among TonB-dependent colicins and receptors.";
RL J. Bacteriol. 169:3350-3357(1987).
CC -!- FUNCTION: This colicin is a channel-forming colicin. This class of
CC transmembrane toxins depolarize the cytoplasmic membrane, leading to
CC dissipation of cellular energy.
CC -!- FUNCTION: Colicins are polypeptide toxins produced by and active
CC against E.coli and closely related bacteria.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: This colicin requires TonB for its uptake.
CC -!- SIMILARITY: Belongs to the channel forming colicin family.
CC {ECO:0000305}.
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DR EMBL; M16816; AAA98063.1; -; Genomic_DNA.
DR PIR; A27089; IKECBB.
DR RefSeq; WP_001282376.1; NZ_WVVE01000043.1.
DR RefSeq; YP_008998007.1; NC_023315.1.
DR PDB; 1RH1; X-ray; 2.50 A; A=2-511.
DR PDBsum; 1RH1; -.
DR AlphaFoldDB; P05819; -.
DR SMR; P05819; -.
DR TCDB; 1.C.1.3.2; the channel-forming colicin (colicin) family.
DR EvolutionaryTrace; P05819; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:InterPro.
DR Gene3D; 1.10.490.30; -; 1.
DR InterPro; IPR000293; Channel_colicin_C.
DR InterPro; IPR038283; Channel_colicin_C_sf.
DR InterPro; IPR016128; Pyosin/cloacin_T_dom.
DR InterPro; IPR036302; Pyosin/cloacin_T_dom_sf.
DR Pfam; PF03515; Cloacin; 1.
DR Pfam; PF01024; Colicin; 1.
DR PRINTS; PR00280; CHANLCOLICIN.
DR SUPFAM; SSF69369; SSF69369; 1.
DR PROSITE; PS00276; CHANNEL_COLICIN; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin; Cell membrane;
KW Direct protein sequencing; Membrane; Plasmid; TonB box; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..511
FT /note="Colicin-B"
FT /id="PRO_0000218687"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 17..24
FT /note="TonB box"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1RH1"
FT TURN 74..81
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 161..176
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 179..196
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:1RH1"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 291..340
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 342..357
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 366..376
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 386..398
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 401..406
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 420..435
FT /evidence="ECO:0007829|PDB:1RH1"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 441..452
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 457..472
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 479..495
FT /evidence="ECO:0007829|PDB:1RH1"
FT HELIX 500..508
FT /evidence="ECO:0007829|PDB:1RH1"
SQ SEQUENCE 511 AA; 54863 MW; 8ABB972CF1925964 CRC64;
MSDNEGSVPT EGIDYGDTMV VWPSTGRIPG GDVKPGGSSG LAPSMPPGWG DYSPQGIALV
QSVLFPGIIR RIILDKELEE GDWSGWSVSV HSPWGNEKVS AARTVLENGL RGGLPEPSRP
AAVSFARLEP ASGNEQKIIR LMVTQQLEQV TDIPASQLPA AGNNVPVKYR LTDLMQNGTQ
YMAIIGGIPM TVPVVDAVPV PDRSRPGTNI KDVYSAPVSP NLPDLVLSVG QMNTPVRSNP
EIQEDGVISE TGNYVEAGYT MSSNNHDVIV RFPEGSGVSP LYISAVEILD SNSLSQRQEA
ENNAKDDFRV KKEQENDEKT VLTKTSEVII SVGDKVGEYL GDKYKALSRE IAENINNFQG
KTIRSYDDAM SSINKLMANP SLKINATDKE AIVNAWKAFN AEDMGNKFAA LGKTFKAADY
AIKANNIREK SIEGYQTGNW GPLMLEVESW VISGMASAVA LSLFSLTLGS ALIAFGLSAT
VVGFVGVVIA GAIGAFIDDK FVDELNHKII K
