AFTD_MYCS2
ID AFTD_MYCS2 Reviewed; 1414 AA.
AC A0QPD4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Alpha-(1->3)-arabinofuranosyltransferase;
DE EC=2.4.2.47;
DE AltName: Full=Arabinofuranan 3-O-arabinosyltransferase;
GN Name=aftD; OrderedLocusNames=MSMEG_0359, MSMEI_0352;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=19654261; DOI=10.1093/glycob/cwp116;
RA Skovierova H., Larrouy-Maumus G., Zhang J., Kaur D., Barilone N.,
RA Kordulakova J., Gilleron M., Guadagnini S., Belanova M., Prevost M.C.,
RA Gicquel B., Puzo G., Chatterjee D., Brennan P.J., Nigou J., Jackson M.;
RT "AftD, a novel essential arabinofuranosyltransferase from mycobacteria.";
RL Glycobiology 19:1235-1247(2009).
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. {ECO:0000269|PubMed:19654261}.
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:19654261};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show cell death, a
CC decrease in its activity, defects in cell division, reduced growth,
CC alteration of colonial morphology, and accumulation of trehalose
CC dimycolates in the cell envelope. {ECO:0000269|PubMed:19654261}.
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DR EMBL; CP000480; ABK71542.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36833.1; -; Genomic_DNA.
DR RefSeq; YP_884772.1; NC_008596.1.
DR AlphaFoldDB; A0QPD4; -.
DR SMR; A0QPD4; -.
DR STRING; 246196.MSMEI_0352; -.
DR PRIDE; A0QPD4; -.
DR EnsemblBacteria; ABK71542; ABK71542; MSMEG_0359.
DR EnsemblBacteria; AFP36833; AFP36833; MSMEI_0352.
DR KEGG; msg:MSMEI_0352; -.
DR KEGG; msm:MSMEG_0359; -.
DR PATRIC; fig|246196.19.peg.356; -.
DR eggNOG; COG4981; Bacteria.
DR OMA; AYGYFFP; -.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR021798; AftD.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR Pfam; PF11847; DUF3367; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1414
FT /note="Alpha-(1->3)-arabinofuranosyltransferase"
FT /id="PRO_0000420583"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1253..1273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1297..1317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1333..1353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1364..1384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 687..845
FT /note="F5/8 type C"
FT REGION 1393..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1414 AA; 148378 MW; 8CB4F189B70B9E36 CRC64;
MVAAATLVLT FAQSPGQISP DTKLDLTANP LRFLARAFNL WNSDLPFGQA QNQAYGYLFP
HGTFFLLGDV LGVPGWVTQR LWWALLLTVG FWGVLRVAEA LGIGSTPSRL IGAAAFALSP
RVLTTLGAIS SETLPMMLAP WVLLPVILAL RGQHSVRLMA ARSAGAVALM GAVNAVATLT
GCLAAVIWWA CHRPNRLWWR FTAWWLLCGA LAVTWWVVAL LMLGRISPPF LDFIESSGVT
TQWMSLTEML RGTMSWTPFV APSATAGASL VTSTTAVLAT TVVAAAGLAG LALRTMPARG
RLITMLLIGV VLLGLGYSGG LGSPVALQVQ AFLDGSGTPL RNLAKLEPVI RLPLALGLVH
LLGRIPLPGS APRAVWVSAF AHPERDKRVA VAIVVLSALA AGTSLAWTAR LTPPGSFTAI
PQHWHDAAAW LDEHNTDRGR VLVAPGAPFA TQVWGNSHDE PLQVLGDNPW GVRDSIPLTP
PETIRALDSV QRLFASGRPS PGLADTLARQ GISYVVVRND LDPDTSRSAR PILVHRAVEG
SPGLTKVAEF GDPVGPGTLE GFVADSGLRP RYPAVEIFRV EPADAGSSQQ RSPMHPYLVD
SDAMTRVAGA PEALLRLDER RRLNGEPPLG PMLLAADARR AGLPVDGVIV TDTPTAREID
YGRVDDHASA IRTPDDARHT YNRVPDYPSD GADLVYGKWT GGRLSVSSSA ADSTALPYVA
PATGPAAAID SDSSTAWVSN ALQAAVGQWL QVDFDHPVTN ATLTITPSAT AVGAQVRRIE
IATATGTSSL RFDTAGKPLT IPLPVGETPW VRVTAVATDD GSPGVQFGVT DLAITQYDAS
GFAHPVTLRH TVEVPGPPAG SVVQQWDLGT ELLGRPGCAD SPVGVRCAAA MALASEEPVN
LSRTLTVPQD TEVQPTVWIR GRQGPNLADL VAQPDTTRAF GDSDPIDVLG SAYAATDGDP
RTSWTAPQRV VQFQTPPTLT LKLPRPTEVS GMRIVPGDTE PPAHPTLVAI DLGDGPQMHR
LPADGEPRTV TLKPRVTDTV TVSLLAWNDI IDRTSLGFDQ LKPPGLAELT VLDGRGAPVG
AADAAKNRSR AVALPCGQGP IIAVAGQFIQ TSVHTTVGAL LDGEPIPARP CRSEPVKLPA
GQQELVVSPG AAFIVDGVEL PTPAADEIRS APTTSAETGT WTADRREVRV SAAAQQRVLV
VPESVNRGWS AHDPAGAELQ SVTVNGWQQG WVVPAGTEGT VTLTFASNMP YRVGLIGGLA
LLPLLALLAL IPVRRPVRAA APARPWNPGP VLTGAAALVA GTAISGVAGL LVVGAAMGVR
ILLNRRGAAG EKVWDNVTVV VAAGGLILAG SVLSQYPWRS VDGYVGHTPG VQFLALLSVA
FLAASAVRLV NRPEPSEDGR SAKPEHTGAS AHAG
