AFTA_MYCTO
ID AFTA_MYCTO Reviewed; 643 AA.
AC P9WN02; L0TGK7; P72058; Q8VIT6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
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=MT3899.1;
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 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 It is not able to add an Araf residue to a terminal Galf.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK48265.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK48265.1; ALT_FRAME; Genomic_DNA.
DR PIR; D70697; D70697.
DR RefSeq; WP_003899694.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WN02; -.
DR CAZy; GT85; Glycosyltransferase Family 85.
DR EnsemblBacteria; AAK48265; AAK48265; MT3899.1.
DR KEGG; mtc:MT3899.1; -.
DR PATRIC; fig|83331.31.peg.4196; -.
DR HOGENOM; CLU_021304_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: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; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..643
FT /note="Galactan 5-O-arabinofuranosyltransferase"
FT /id="PRO_0000427212"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..643
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 643 AA; 69515 MW; 7C58972B085D9EDA CRC64;
MPSRRKSPQF GHEMGAFTSA RAREVLVALG QLAAAVVVAV GVAVVSLLAI ARVEWPAFPS
SNQLHALTTV GQVGCLAGLV GIGWLWRHGR FRRLARLGGL VLVSAFTVVT LGMPLGATKL
YLFGISVDQQ FRTEYLTRLT DTAALRDMTY IGLPPFYPPG WFWIGGRAAA LTGTPAWEMF
KPWAITSMAI AVAVALVLWW RMIRFEYALL VTVATAAVML AYSSPEPYAA MITVLLPPML
VLTWSGLGAR DRQGWAAVVG AGVFLGFAAT WYTLLVAYGA FTVVLMALLL AGSRLQSGIK
AAVDPLCRLA VVGAIAAAIG STTWLPYLLR AARDPVSDTG SAQHYLPADG AALTFPMLQF
SLLGAICLLG TLWLVMRARS SAPAGALAIG VLAVYLWSLL SMLATLARTT LLSFRLQPTL
SVLLVAAGAF GFVEAVQALG KRGRGVIPMA AAIGLAGAIA FSQDIPDVLR PDLTIAYTDT
DGYGQRGDRR PPGSEKYYPA IDAAIRRVTG KRRDRTVVLT ADYSFLSYYP YWGFQGLTPH
YANPLAQFDK RATQIDSWSG LSTADEFIAA LDKLPWQPPT VFLMRHGAHN SYTLRLAQDV
YPNQPNVRRY TVDLRTALFA DPRFVVEDIG PFVLAIRKPQ ESA
