MCBC_ECOLX
ID MCBC_ECOLX Reviewed; 272 AA.
AC P23185;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Microcin B17-processing protein McbC;
GN Name=mcbC;
OS Escherichia coli.
OG Plasmid IncFII pMccB17.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2644225; DOI=10.1128/jb.171.2.1126-1135.1989;
RA Genilloud O., Moreno F., Kolter R.;
RT "DNA sequence, products, and transcriptional pattern of the genes involved
RT in production of the DNA replication inhibitor microcin B17.";
RL J. Bacteriol. 171:1126-1135(1989).
CC -!- FUNCTION: Necessary to process the inactive microcin B17 (McbA)
CC precursor into the active peptide.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: To R.leguminosarum TfxB which is involved in the processing
CC of trifolitoxin. {ECO:0000305}.
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DR EMBL; M24253; AAA72743.1; -; Genomic_DNA.
DR PIR; C32058; C32058.
DR RefSeq; WP_001528601.1; NZ_WSWV01000078.1.
DR PDB; 6GOS; X-ray; 2.10 A; C=1-272.
DR PDB; 6GRG; X-ray; 2.35 A; C=1-272.
DR PDB; 6GRH; X-ray; 1.85 A; C=1-272.
DR PDB; 6GRI; X-ray; 2.70 A; C=1-272.
DR PDBsum; 6GOS; -.
DR PDBsum; 6GRG; -.
DR PDBsum; 6GRH; -.
DR PDBsum; 6GRI; -.
DR AlphaFoldDB; P23185; -.
DR SMR; P23185; -.
DR BioCyc; MetaCyc:MON-21088; -.
DR BRENDA; 1.3.3.16; 2026.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR InterPro; IPR020051; SagB-type_dehydrogenase.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
DR TIGRFAMs; TIGR03605; antibiot_sagB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Cytoplasm; Plasmid.
FT CHAIN 1..272
FT /note="Microcin B17-processing protein McbC"
FT /id="PRO_0000068572"
FT HELIX 8..12
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:6GRH"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6GRH"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6GRH"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:6GRH"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6GRH"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:6GRH"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:6GRH"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:6GRH"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 204..227
FT /evidence="ECO:0007829|PDB:6GRH"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:6GRH"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:6GRH"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:6GRH"
SQ SEQUENCE 272 AA; 30753 MW; 956E1744338C051D CRC64;
MSKHELSLVE VTHYTDPEVL AIVKDFHVRG NFASLPEFAE RTFVSAVPLA HLEKFENKEV
LFRPGFSSVI NISSSHNFSR ERLPSGINFC DKNKLSIRTI EKLLVNAFSS PDPGSVRRPY
PSGGALYPIE VFLCRLSENT ENWQAGTNVY HYLPLSQALE PVATCNTQSL YRSLSGGDSE
RLGKPHFALV YCIIFEKALF KYRYRGYRMA LMETGSMYQN AVLVADQIGL KNRVWAGYTD
SYVAKTMNLD QRTVAPLIVQ FFGDVNDDKC LQ