ID   MFTB_MYCS2              Reviewed;         102 AA.
AC   A0QSB7;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Peptide chaperone MftB {ECO:0000305};
GN   Name=mftB {ECO:0000303|PubMed:27158836};
GN   OrderedLocusNames=MSMEG_1422 {ECO:0000312|EMBL:ABK73646.1};
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=27158836; DOI=10.1021/acs.biochem.6b00355;
RA   Bruender N.A., Bandarian V.;
RT   "The Radical S-Adenosyl-L-methionine Enzyme MftC Catalyzes an Oxidative
RT   Decarboxylation of the C-Terminus of the MftA Peptide.";
RL   Biochemistry 55:2813-2816(2016).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=31113891; DOI=10.1128/mbio.00190-19;
RA   Krishnamoorthy G., Kaiser P., Lozza L., Hahnke K., Mollenkopf H.J.,
RA   Kaufmann S.H.E.;
RT   "Mycofactocin Is Associated with Ethanol Metabolism in Mycobacteria.";
RL   MBio 10:E00190-E00190(2019).
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 (PubMed:27158836) (By similarity). Is required for
CC       the in vivo ethanol assimilation in M.smegmatis (PubMed:31113891).
CC       {ECO:0000250|UniProtKB:A0PM48, ECO:0000269|PubMed:27158836,
CC       ECO:0000269|PubMed:31113891}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to
CC       utilize ethanol as the sole growth substrate.
CC       {ECO:0000269|PubMed:31113891}.
CC   -!- SIMILARITY: Belongs to the peptide chaperone MftB family.
CC       {ECO:0000305}.
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DR   EMBL; CP000480; ABK73646.1; -; Genomic_DNA.
DR   RefSeq; WP_003892808.1; NZ_SIJM01000016.1.
DR   RefSeq; YP_885805.1; NC_008596.1.
DR   AlphaFoldDB; A0QSB7; -.
DR   SMR; A0QSB7; -.
DR   STRING; 246196.MSMEI_1387; -.
DR   EnsemblBacteria; ABK73646; ABK73646; MSMEG_1422.
DR   GeneID; 66732881; -.
DR   KEGG; msm:MSMEG_1422; -.
DR   PATRIC; fig|246196.19.peg.1409; -.
DR   eggNOG; COG0535; Bacteria.
DR   OMA; QGPYLHA; -.
DR   OrthoDB; 2043869at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   InterPro; IPR023850; MftB.
DR   TIGRFAMs; TIGR03967; mycofact_MftB; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..102
FT                   /note="Peptide chaperone MftB"
FT                   /id="PRO_0000452058"
SQ   SEQUENCE   102 AA;  11134 MW;  8401ED7842AA5195 CRC64;
     MSTQVAEQIT FDPDVSWRLH HQVAVRPEPF GALLYHFGTR KLSFLKNRTV VEVVNSLADH
     PDARSALCAA GVADDQQAPY LHALGVLVQS NMLVPGNPEG SQ