AFTC_MYCTU
ID AFTC_MYCTU Reviewed; 433 AA.
AC P9WMZ7; F2GLI3; L0TAJ6; P71970; Q7D6S9;
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=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=Rv2673;
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, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND NOMENCLATURE.
RX PubMed=18627460; DOI=10.1111/j.1365-2958.2008.06354.x;
RA Birch H.L., Alderwick L.J., Bhatt A., Rittmann D., Krumbach K., Singh A.,
RA Bai Y., Lowary T.L., Eggeling L., Besra G.S.;
RT "Biosynthesis of mycobacterial arabinogalactan: identification of a novel
RT alpha(1-->3) arabinofuranosyltransferase.";
RL Mol. Microbiol. 69:1191-1206(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=21595486; DOI=10.1021/cb200091m;
RA Zhang J., Angala S.K., Pramanik P.K., Li K., Crick D.C., Liav A.,
RA Jozwiak A., Swiezewska E., Jackson M., Chatterjee D.;
RT "Reconstitution of functional mycobacterial arabinosyltransferase AftC
RT proteoliposome and assessment of decaprenylphosphorylarabinose analogues as
RT arabinofuranosyl donors.";
RL ACS Chem. Biol. 6:819-828(2011).
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).
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 decaprenyl-phospho-arabinose (DPA) on the C-3 of an alpha-(1->5)-linked
CC Araf from the arabinan backbone of AG. It can also use (Z,Z)-
CC farnesylphosphoryl D-arabinose (Z-FPA), and to a lesser extent
CC (E,E,Z,Z,Z,Z)-heptaprenylphosphoryl D-arabinose (Z-HPA) and (Z)-
CC nerylphosphoryl D-arabinose (Z-NPA) as sugar donors.
CC {ECO:0000269|PubMed:18627460, ECO:0000269|PubMed:21595486}.
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 Evidence={ECO:0000269|PubMed:18627460, ECO:0000269|PubMed:21595486};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene result in an increased
CC permeability and an altered cell wall. {ECO:0000269|PubMed:18627460}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 87 family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45471.1; -; Genomic_DNA.
DR PIR; E70968; E70968.
DR RefSeq; NP_217189.1; NC_000962.3.
DR AlphaFoldDB; P9WMZ7; -.
DR STRING; 83332.Rv2673; -.
DR PaxDb; P9WMZ7; -.
DR DNASU; 887396; -.
DR GeneID; 887396; -.
DR KEGG; mtu:Rv2673; -.
DR TubercuList; Rv2673; -.
DR eggNOG; ENOG5033U55; Bacteria.
DR OMA; AMFCTES; -.
DR BioCyc; MetaCyc:G185E-6921-MON; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001584; 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 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..433
FT /note="Alpha-(1->3)-arabinofuranosyltransferase"
FT /id="PRO_0000420579"
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