ID   AFTC_MYCTO              Reviewed;         433 AA.
AC   P9WMZ6; F2GLI3; L0TAJ6; P71970; Q7D6S9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Alpha-(1->3)-arabinofuranosyltransferase;
DE            EC=2.4.2.47;
DE   AltName: Full=Arabinofuranan 3-O-arabinosyltransferase;
DE   AltName: Full=Arabinofuranosyltransferase C;
GN   Name=aftC; OrderedLocusNames=MT2747;
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 arabinogalactan (AG)
CC       region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an
CC       essential component of the mycobacterial cell wall. Catalyzes the
CC       addition of an arabinofuranosyl (Araf) residue from the sugar donor
CC       beta-D-arabinofuranosyl-1-monophosphoryldecaprenol (DPA) on the C-3 of
CC       an alpha-(1->5)-linked Araf from the arabinan backbone of AG.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Adds an alpha-D-arabinofuranosyl group from trans,octacis-
CC         decaprenylphospho-beta-D-arabinofuranose at the 3-O-position of an
CC         alpha-(1->5)-arabinofuranan chain attached to a beta-(1->5)-
CC         galactofuranan chain.; EC=2.4.2.47;
CC   -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 87 family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47062.1; -; Genomic_DNA.
DR   PIR; E70968; E70968.
DR   AlphaFoldDB; P9WMZ6; -.
DR   EnsemblBacteria; AAK47062; AAK47062; MT2747.
DR   KEGG; mtc:MT2747; -.
DR   PATRIC; fig|83331.31.peg.2958; -.
DR   HOGENOM; CLU_055106_0_0_11; -.
DR   UniPathway; UPA00963; -.
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:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR018584; GT87.
DR   Pfam; PF09594; GT87; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..433
FT                   /note="Alpha-(1->3)-arabinofuranosyltransferase"
FT                   /id="PRO_0000427215"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   433 AA;  48915 MW;  899AB13A4F7946EC CRC64;
     MYGALVTAAD SIRTGLGASL LAGFRPRTGA PSTATILRSA LWPAAVLSVL HRSIVLTTNG
     NITDDFKPVY RAVLNFRRGW DIYNEHFDYV DPHYLYPPGG TLLMAPFGYL PFAPSRYLFI
     SINTAAILVA AYLLLRMFNF TLTSVAAPAL ILAMFATETV TNTLVFTNIN GCILLLEVLF
     LRWLLDGRAS RQWCGGLAIG LTLVLKPLLG PLLLLPLLNR QWRALVAAVV VPVVVNVAAL
     PLVSDPMSFF TRTLPYILGT RDYFNSSILG NGVYFGLPTW LILFLRILFT AITFGALWLL
     YRYYRTGDPL FWFTTSSGVL LLWSWLVMSL AQGYYSMMLF PFLMTVVLPN SVIRNWPAWL
     GVYGFMTLDR WLLFNWMRWG RALEYLKITY GWSLLLIVTF TVLYFRYLDA KADNRLDGGI
     DPAWLTPERE GQR