AFTA_MYCTU
ID AFTA_MYCTU Reviewed; 643 AA.
AC P9WN03; 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 40.
DE RecName: Full=Galactan 5-O-arabinofuranosyltransferase {ECO:0000305};
DE EC=2.4.2.46 {ECO:0000269|PubMed:16595677, ECO:0000305|PubMed:18556798};
DE AltName: Full=Arabinofuranosyltransferase AftA {ECO:0000303|PubMed:16595677};
GN Name=aftA {ECO:0000303|PubMed:16595677}; OrderedLocusNames=Rv3792;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS AN ARABINOFURANOSYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16595677; DOI=10.1074/jbc.m600045200;
RA Alderwick L.J., Seidel M., Sahm H., Besra G.S., Eggeling L.;
RT "Identification of a novel arabinofuranosyltransferase (AftA) involved in
RT cell wall arabinan biosynthesis in Mycobacterium tuberculosis.";
RL J. Biol. Chem. 281:15653-15661(2006).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=H37Rv;
RX PubMed=18556798; DOI=10.1128/jb.00028-08;
RA Shi L., Zhou R., Liu Z., Lowary T.L., Seeberger P.H., Stocker B.L.,
RA Crick D.C., Khoo K.H., Chatterjee D.;
RT "Transfer of the first arabinofuranose residue to galactan is essential for
RT Mycobacterium smegmatis viability.";
RL J. Bacteriol. 190:5248-5255(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP INTERACTION WITH RV3789.
RC STRAIN=H37Rv;
RX PubMed=26369580; DOI=10.1128/jb.00628-15;
RA Kolly G.S., Mukherjee R., Kilacskova E., Abriata L.A., Raccaud M.,
RA Blasko J., Sala C., Dal Peraro M., Mikusova K., Cole S.T.;
RT "GtrA protein Rv3789 is required for arabinosylation of arabinogalactan in
RT Mycobacterium tuberculosis.";
RL J. Bacteriol. 197:3686-3697(2015).
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:0000269|PubMed:16595677, ECO:0000305|PubMed:18556798}.
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:0000269|PubMed:16595677, ECO:0000305|PubMed:18556798};
CC -!- ACTIVITY REGULATION: Not inhibited by the anti-tuberculosis drug
CC ethambutol (EMB). {ECO:0000269|PubMed:16595677}.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:16595677}.
CC -!- SUBUNIT: Interacts with Rv3789. Is thus probably part of an AG
CC biosynthetic complex. {ECO:0000269|PubMed:26369580}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16595677};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16595677}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 85 family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46621.1; -; Genomic_DNA.
DR PIR; D70697; D70697.
DR RefSeq; NP_218309.1; NC_000962.3.
DR RefSeq; WP_003899694.1; NZ_NVQJ01000009.1.
DR AlphaFoldDB; P9WN03; -.
DR STRING; 83332.Rv3792; -.
DR PaxDb; P9WN03; -.
DR GeneID; 886127; -.
DR KEGG; mtu:Rv3792; -.
DR PATRIC; fig|83332.111.peg.4217; -.
DR TubercuList; Rv3792; -.
DR eggNOG; ENOG502ZB59; Bacteria.
DR OMA; YPAGWFW; -.
DR BioCyc; MetaCyc:G185E-8088-MON; -.
DR BRENDA; 2.4.2.46; 3445.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071769; P:mycolate cell wall layer assembly; IMP:MTBBASE.
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 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..643
FT /note="Galactan 5-O-arabinofuranosyltransferase"
FT /id="PRO_0000250356"
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
