ID   MFTF_MYCTO              Reviewed;         470 AA.
AC   P9WMX0; L0T4G0; P95042; Q7D9E7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Pre-mycofactocin glycosyltransferase;
DE            EC=2.4.1.- {ECO:0000250|UniProtKB:A0QSC1};
GN   Name=mftF; OrderedLocusNames=MT0723;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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. Is required for the in vivo ethanol
CC       assimilation in M.smegmatis. {ECO:0000250|UniProtKB:A0QSC1}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44952.1; -; Genomic_DNA.
DR   PIR; C70641; C70641.
DR   RefSeq; WP_003403501.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMX0; -.
DR   SMR; P9WMX0; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; AAK44952; AAK44952; MT0723.
DR   KEGG; mtc:MT0723; -.
DR   PATRIC; fig|83331.31.peg.773; -.
DR   HOGENOM; CLU_028391_0_0_11; -.
DR   Proteomes; UP000001020; 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; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..470
FT                   /note="Pre-mycofactocin glycosyltransferase"
FT                   /id="PRO_0000427228"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   470 AA;  50667 MW;  D2D6AC3F43D77414 CRC64;
     MTATRLPDGF AVQVDRRVRV LGDGSALLGG SPTRLLRLAP AARGLLCDGR LKVRDEVSAE
     LARILLDATV AHPRPPSGPS HRDVTVVIPV RNNASGLRRL VTSLRGLRVI VVDDGSACPV
     ESDDFVGAHC DIEVLHHPHS KGPAAARNTG LAACTTDFVA FLDSDVTPRR GWLESLLGHF
     CDPTVALVAP RIVSLVEGEN PVARYEALHS SLDLGQREAP VLPHSTVSYV PSAAIVCRSS
     AIRDVGGFDE TMHSGEDVDL CWRLIEAGAR LRYEPIALVA HDHRTQLRDW IARKAFYGGS
     AAPLAVRHPD KTAPLVISGG ALMAWILMSI GTGLGRLASL VIAVLTGRRI ARAMRCAETS
     FLDVLAVATR GLWAAALQLA SAICRHYWPL ALLAAILSRR CRRVVLIAAV VDGVVDWLRR
     REGADDDAEP IGPLTYLVLK RVDDLAYGAG LWYGVVRERN IGALKPQIRT