ID   MFTF_MYCS2              Reviewed;         470 AA.
AC   A0QSC1;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Pre-mycofactocin glycosyltransferase {ECO:0000305|PubMed:33014324};
DE            EC=2.4.1.- {ECO:0000305|PubMed:33014324};
GN   Name=mftF {ECO:0000303|PubMed:33014324};
GN   OrderedLocusNames=MSMEG_1426 {ECO:0000312|EMBL:ABK72099.1};
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, 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).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=33014324; DOI=10.1039/d0sc01172j;
RA   Pena-Ortiz L., Graca A.P., Guo H., Braga D., Koellner T.G., Regestein L.,
RA   Beemelmanns C., Lackner G.;
RT   "Structure elucidation of the redox cofactor mycofactocin reveals oligo-
RT   glycosylation by MftF.";
RL   Chem. Sci. 11:5182-5190(2020).
CC   -!- FUNCTION: Involved in the biosynthesis of the enzyme cofactor
CC       mycofactocin (MFT). Acts as a glycosyltransferase that catalyzes the
CC       oligoglycosylation of pre-mycofactocin (PMFT), adding up to nine beta-
CC       1,4-linked glucose residues (PubMed:33014324). Is required for the in
CC       vivo ethanol assimilation in M.smegmatis (PubMed:31113891).
CC       {ECO:0000269|PubMed:31113891, ECO:0000269|PubMed:33014324}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to
CC       utilize ethanol as the sole growth substrate (PubMed:31113891).
CC       Glycosylated mycofactocins are not detected in this mutant, as well as
CC       PMFT and PMFTH(2) (PubMed:33014324). {ECO:0000269|PubMed:31113891,
CC       ECO:0000269|PubMed:33014324}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; CP000480; ABK72099.1; -; Genomic_DNA.
DR   RefSeq; WP_011727662.1; NZ_SIJM01000016.1.
DR   RefSeq; YP_885809.1; NC_008596.1.
DR   AlphaFoldDB; A0QSC1; -.
DR   SMR; A0QSC1; -.
DR   STRING; 246196.MSMEI_1391; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ABK72099; ABK72099; MSMEG_1426.
DR   GeneID; 66732885; -.
DR   KEGG; msm:MSMEG_1426; -.
DR   PATRIC; fig|246196.19.peg.1413; -.
DR   eggNOG; COG1216; Bacteria.
DR   OMA; HVAHDHR; -.
DR   OrthoDB; 1445278at2; -.
DR   BioCyc; MetaCyc:MON-21109; -.
DR   Proteomes; UP000000757; Chromosome.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR023981; MftF.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43646:SF6; PTHR43646:SF6; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03965; mycofact_glyco; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..470
FT                   /note="Pre-mycofactocin glycosyltransferase"
FT                   /id="PRO_0000452055"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   470 AA;  50477 MW;  E99F0E09690595F2 CRC64;
     MTGPRLPDGF AVQVDRRVKV LGEGAALLGG SPTRLLRLAP TAQNMLSGGR LEVHDAVSAQ
     LARTLLDATV AHPRPASGPS HLDVTVVVPV RDNASGLHRL MAALRGLRVI VVDDGSAIPV
     QPSDFSGMHC DVQVLRHTRS NGPAAARNTG LASCETDFVA FLDSDVVPKR GWLEALLGHF
     CDPAVALVAP RIVGLHNADN IVARYESVRS SLDLGVREAP VVPHGTVSYV PSAAIICRRS
     ALVEVGGFDE TMHSGEDVDL CWRLVESGAR LRYEPIALVA HDHRTNLRAW FHRKAFYGTS
     AAPLTVRHPG KTSPLVISGW TLMVWLMLGV GSFFGYLASL AAAVFAGTRI ARALSVVETE
     PKEVAVVAAH GLWSSALQLC SAICRHYWPI AMIAAVLFRR ARHAVLVAAV VDGVVDWVTR
     RGNADDDTKP VGLLTHIVLK RLDDIAYGTG LWTGVVRERH LGALKPQVRS