ID   AFTA_MYCLE              Reviewed;         632 AA.
AC   Q9CDA6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Galactan 5-O-arabinofuranosyltransferase {ECO:0000250|UniProtKB:P9WN03};
DE            EC=2.4.2.46 {ECO:0000250|UniProtKB:P9WN03};
DE   AltName: Full=Arabinofuranosyltransferase AftA {ECO:0000250|UniProtKB:P9WN03};
GN   Name=aftA {ECO:0000250|UniProtKB:P9WN03}; OrderedLocusNames=ML0107;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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 the first key arabinofuranosyl (Araf) residue from the
CC       sugar donor decaprenyl-phospho-arabinose (DPA) on the C-5 of a 6-linked
CC       galactofuranosyl (Galf) of the galactan domain, thus 'priming' the
CC       galactan for further elaboration by other arabinofuranosyltransferases.
CC       {ECO:0000250|UniProtKB:P9WN03}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Adds an alpha-D-arabinofuranosyl group from trans,octacis-
CC         decaprenylphospho-beta-D-arabinofuranose at the 5-O-position of the
CC         eighth, tenth and twelfth galactofuranose unit of the galactofuranan
CC         chain of [beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-
CC         (1->6)]14-beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-
CC         (1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-
CC         diphospho-trans,octacis-decaprenol.; EC=2.4.2.46;
CC         Evidence={ECO:0000250|UniProtKB:P9WN03};
CC   -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WN03}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WN03};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P9WN03}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 85 family.
CC       {ECO:0000305}.
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DR   EMBL; AL583917; CAC29615.1; -; Genomic_DNA.
DR   PIR; C86922; C86922.
DR   RefSeq; NP_301204.1; NC_002677.1.
DR   RefSeq; WP_010907529.1; NC_002677.1.
DR   AlphaFoldDB; Q9CDA6; -.
DR   STRING; 272631.ML0107; -.
DR   CAZy; GT85; Glycosyltransferase Family 85.
DR   EnsemblBacteria; CAC29615; CAC29615; CAC29615.
DR   KEGG; mle:ML0107; -.
DR   PATRIC; fig|272631.5.peg.170; -.
DR   Leproma; ML0107; -.
DR   eggNOG; ENOG502ZB59; Bacteria.
DR   HOGENOM; CLU_021304_0_0_11; -.
DR   OMA; YPAGWFW; -.
DR   UniPathway; UPA00963; -.
DR   Proteomes; UP000000806; 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   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR020959; ArabinofuranosylTrfase_AftA_C.
DR   InterPro; IPR020963; ArabinofuranosylTrfase_AftA_N.
DR   Pfam; PF12249; AftA_C; 1.
DR   Pfam; PF12250; AftA_N; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..632
FT                   /note="Galactan 5-O-arabinofuranosyltransferase"
FT                   /id="PRO_0000250355"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        455..632
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   632 AA;  68650 MW;  48BA01D7CFB252CE CRC64;
     MRNALASFGQ IVLAAVVASG VAAVSLIAIA RVHWPAFPSS NQLHALTTVG QVGCLTGLLA
     VGGVWQAGRF RRLAQLGGLV FVSAFTVVTL GMPLGATKLY LFGISVDQQF RTEYLTRLTD
     SAALQDMTYL GLPPFYPPGW FWIGGRVAAL TGTPAWEIFK PWAITSITIA VAITLVLWWQ
     MIRFEYALLV TIATAAVTLV YSSPEPYAAM ITVLLPPALV LTWSGLRAAE READRTLGNK
     RGWATVVGAG IFLGFAATWY TLLLAYTAFT VVLMTLLLAT ALCRRAGFRA TFDPLRRLAG
     IVVIAAAIGA ITWLPFLARA AHDPVSDTGS AQHYLPADGA ELAFPMLQFS LLGMICMLGT
     LWLIVRTSSS VRASALMISV LAVYLWSLLS ILTTLARTTL LSFRLQPTLT VLLVTAGVFG
     FIETAQSLAK HNRAVLSVAS AIGLAGAIAF SQDIPNVLRP DLTIAYTDTD GHGQRGDRRP
     PGSEKYYWAI DEAVLHITGK PRDQTVVLTA DYSFLAYYPY WGFQGLTSHY ANPLAQFDLR
     AAQIQQWSRL TTASELIHAL DTLPWPPPTV FVMRHGAGNT YTLRLAKNVY PNQPNVRRYT
     VDLPAALFAD QRFAVQDIGP FVLAIRKPMG NA