AFTC_MYCS2
ID AFTC_MYCS2 Reviewed; 430 AA.
AC A0QW28;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=MSMEG_2785, MSMEI_2716;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
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).
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:0000269|PubMed:18627460}.
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};
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 colonies with a
CC more erose appearance compared with the usual glossy appearance. The
CC mutant yields arabinogalactan (AG) with a significant reduction in
CC arabinofuranosyl (Araf) content concomitant with a relative increase in
CC the amount of galactanfuranosyl (Galf). It shows only a slightly
CC reduced growth rate. {ECO:0000269|PubMed:18627460}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 87 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK72123.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39184.1; -; Genomic_DNA.
DR RefSeq; YP_887116.1; NC_008596.1.
DR AlphaFoldDB; A0QW28; -.
DR STRING; 246196.MSMEI_2716; -.
DR PRIDE; A0QW28; -.
DR EnsemblBacteria; ABK72123; ABK72123; MSMEG_2785.
DR EnsemblBacteria; AFP39184; AFP39184; MSMEI_2716.
DR KEGG; msg:MSMEI_2716; -.
DR KEGG; msm:MSMEG_2785; -.
DR PATRIC; fig|246196.19.peg.2753; -.
DR eggNOG; ENOG5033U55; Bacteria.
DR OMA; AMFCTES; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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..430
FT /note="Alpha-(1->3)-arabinofuranosyltransferase"
FT /id="PRO_0000420580"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 430 AA; 48768 MW; 22B0B72DDDA85442 CRC64;
MYCALVTATD SITTKLLNAF RPRTSAPSTA TVLRSVLWPI AILSVIHRSY VLGTNGYITD
DFGPVYRAVI NFKLGLDIYN EQFDHVDPHY LYPPGGTLLL APFGYLPVDA SRYWYISFNV
LAFLIAAYLM LRIFDYTLSS VAAPALVLAM FCTESVTNTL VFTNINGCML LGAVLFFRWL
LKGGRNAELL AGAAIGLTLV VKPSLAPLLL LPVLNRQFYT LITAFGVPLV FNIAAWPLVP
DPMNFVRHTV PYIMSTRDYF NSSIVGNGIY YGLPMWLILL LRVVFLLLAV GSLWLLYRYY
RERDPRFWLL TSSGVLLTAS FLLLSLGQGY YSTMLFPFLM TVVLPNSVLR NWPAWLAIYG
FMTMDRWLLG HWPTTGRFLE YMKITYGWSL MLVVVFCVLY FRYLDAKQDG RLDQGIDPPW
MARERTPAPV
