ID   MFTB_MYCUA              Reviewed;         109 AA.
AC   A0PM48;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Peptide chaperone MftB {ECO:0000303|PubMed:27312813};
GN   Name=mftB {ECO:0000303|PubMed:27312813, ECO:0000303|PubMed:28634235};
GN   OrderedLocusNames=MUL_0772 {ECO:0000312|EMBL:ABL03417.1};
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH MFTA AND MFTC.
RX   PubMed=27312813; DOI=10.1002/1873-3468.12249;
RA   Khaliullin B., Aggarwal P., Bubas M., Eaton G.R., Eaton S.S., Latham J.A.;
RT   "Mycofactocin biosynthesis: modification of the peptide MftA by the radical
RT   S-adenosylmethionine protein MftC.";
RL   FEBS Lett. 590:2538-2548(2016).
RN   [3]
RP   FUNCTION.
RC   STRAIN=Agy99;
RX   PubMed=28634235; DOI=10.1074/jbc.m117.795682;
RA   Khaliullin B., Ayikpoe R., Tuttle M., Latham J.A.;
RT   "Mechanistic elucidation of the mycofactocin-biosynthetic radical S-
RT   adenosylmethionine protein, MftC.";
RL   J. Biol. Chem. 292:13022-13033(2017).
CC   -!- FUNCTION: Peptide chaperone involved in the biosynthesis of the enzyme
CC       cofactor mycofactocin (MFT). Binds MftA and MftC with high affinity,
CC       and is essential for MftC activity on MftA, likely via the formation of
CC       a ternary complex. {ECO:0000269|PubMed:27312813}.
CC   -!- SUBUNIT: Interacts with MftA and MftC. {ECO:0000269|PubMed:27312813}.
CC   -!- SIMILARITY: Belongs to the peptide chaperone MftB family.
CC       {ECO:0000305}.
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DR   EMBL; CP000325; ABL03417.1; -; Genomic_DNA.
DR   RefSeq; WP_011739042.1; NC_008611.1.
DR   AlphaFoldDB; A0PM48; -.
DR   SMR; A0PM48; -.
DR   STRING; 362242.MUL_0772; -.
DR   EnsemblBacteria; ABL03417; ABL03417; MUL_0772.
DR   KEGG; mul:MUL_0772; -.
DR   eggNOG; COG0535; Bacteria.
DR   HOGENOM; CLU_159310_1_0_11; -.
DR   OMA; QGPYLHA; -.
DR   BioCyc; MetaCyc:MON-21113; -.
DR   Proteomes; UP000000765; Chromosome.
DR   InterPro; IPR023850; MftB.
DR   TIGRFAMs; TIGR03967; mycofact_MftB; 1.
PE   1: Evidence at protein level;
FT   CHAIN           1..109
FT                   /note="Peptide chaperone MftB"
FT                   /id="PRO_0000452059"
SQ   SEQUENCE   109 AA;  11675 MW;  89A61732590E4166 CRC64;
     MRGLLTVPAP AQAAAGAGAF DPDRGWRLHA QVAVRPEPFG ALLYHFGTRK LSFLKNRTIL
     AVVRSLADHP DVRSACRAAG VDDSEHAPYL HALSVLAGSH MLVPQEADQ