ID   AFTD_MYCTU              Reviewed;        1400 AA.
AC   P96419; L0T2X2;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Alpha-(1->3)-arabinofuranosyltransferase;
DE            EC=2.4.2.47;
DE   AltName: Full=Arabinofuranan 3-O-arabinosyltransferase;
DE   Flags: Precursor;
GN   Name=aftD; OrderedLocusNames=Rv0236c;
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   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. {ECO:0000250}.
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   -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AL123456; CCP42964.1; -; Genomic_DNA.
DR   PIR; B70963; B70963.
DR   RefSeq; NP_214750.1; NC_000962.3.
DR   AlphaFoldDB; P96419; -.
DR   SMR; P96419; -.
DR   STRING; 83332.Rv0236c; -.
DR   PaxDb; P96419; -.
DR   GeneID; 886707; -.
DR   KEGG; mtu:Rv0236c; -.
DR   PATRIC; fig|83332.111.peg.268; -.
DR   TubercuList; Rv0236c; -.
DR   eggNOG; COG4981; Bacteria.
DR   OMA; AYGYFFP; -.
DR   PhylomeDB; P96419; -.
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; HDA:MTBBASE.
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; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   Pfam; PF11847; DUF3367; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   1: Evidence at protein level;
KW   Membrane; Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..1400
FT                   /note="Alpha-(1->3)-arabinofuranosyltransferase"
FT                   /id="PRO_0000420582"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1256..1276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1297..1317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1338..1358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1369..1389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          700..883
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
SQ   SEQUENCE   1400 AA;  146280 MW;  0EBC23F02DE74B59 CRC64;
     MAPLSRKWLP VVGAVALALT FAQSPGQVSP DTKLDLTANP LRFLARATNL WNSDLPFGQA
     QNQAYGYLFP HGTFFVIGHL LGVPGWVTQR LWWAVLLTVG FWGLLRVAEA LGVGGPSSRV
     VGAVAFALSP RVLTTLGSIS SETLPMMLAP WVLLPTILAL RGTSGRSVRA LAAQAGLAVA
     LMGAVNAIAT LAGCLPAVIW WACHRPNRLW WRYTAWWLLA MALATLWWVM ALTQLHGVSP
     PFLDFIESSG VTTQWSSLVE VLRGTDSWTP FVAPNATAGA PLVTGSAAIL GTCLVAAAGL
     AGLTSPAMPA RGRLVTMLLV GVVLLAVGHR GGLASPVAHP VQAFLDAAGT PLRNVHKVGP
     VIRLPLVLGL AQLLSRVPLP GSAPRPAWLR AFAHPERDKR VAVAVVALTA LMVSTSLAWT
     GRVAPPGTFG ALPQYWQEAA DWLRTHHAAT PTPGRVLVVP GAPFATQVWG TSHDEPLQVL
     GDGPWGVRDS IPLTPPQTIR ALDSVQRLFA AGRPSAGLAD TLARQGISYV LVRNDLDPET
     SRSARPILLH RSIAGSPGLA KLAEFGAPVG PDPLAGFVND SGLRPRYPAI EIYRVSAPAN
     PGAPYFAATD QLARVDGGPE VLLRLDERRR LQGQPPLGPV LMTADARAAG LPVPQVAVTD
     TPVARETDYG RVDHHSSAIR APGDARHTYN RVPDYPVPGA EPVVGGWTGG RITVSSSSAD
     ATAMPDVAPA SAPAAAVDGD PATAWVSNAL QAAVGQWLQV DFDRPVTNAV VTLTPSATAV
     GAQVRRILIE TVNGSTTLRF DEAGKPLTAA LPYGETPWVR FTAAATDDGS AGVQFGITDL
     AITQYDASGF AHPVQLRHTV LVPGPPPGSA IAGWDLGSEL LGRPGCAPGP DGVRCAASMA
     LAPEEPANLS RTLTVPRPVS VTPMVWVRPR QGPKLADLIA APSTTRASGD SDLVDILGSA
     YAAADGDPAT AWTAPQRVVQ HKTPPTLTLT LPRPTVVTGL RLAASRSMLP AHPTVVAINL
     GDGPQVRQLQ VGELTTLWLH PRVTDTVSVS LLDWDDVIDR NALGFDQLKP PGLAEVVVLS
     AGGAPIAPAD AARNRARALT VDCDHGPVVA VAGRFVHTSI RTTVGALLDG EPVAALPCER
     EPIALPAGQQ ELLISPGAAF VVDGAQLSTP GAGLSSATVT SAETGAWGPT HREVRVPESA
     TSRVLVVPES INSGWVARTS TGARLTPIAV NGWQQAWVVP AGNPGTITLT FAPNSLYRAS
     LAIGLALLPL LALLAFWRTG RRQLADRPTP PWRPGAWAAA GVLAAGAVIA SIAGVMVMGT
     ALGVRYALRR RERLRDRVTV GLAAGGLILA GAALSRHPWR SVDGYAGNWA SVQLLALISV
     SVVAASVVAT SESRGQDRMQ