ID   EMBA_MYCAV              Reviewed;        1108 AA.
AC   P71485;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Probable arabinosyltransferase A;
DE            EC=2.4.2.-;
GN   Name=embA;
OS   Mycobacterium avium.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2151;
RX   PubMed=8876238; DOI=10.1073/pnas.93.21.11919;
RA   Belanger A.E., Besra G.S., Ford M.E., Mikusova K., Belisle J.T.,
RA   Brennan P.J., Inamine J.M.;
RT   "The embAB genes of Mycobacterium avium encode an arabinosyl transferase
RT   involved in cell wall arabinan biosynthesis that is the target for the
RT   antimycobacterial drug ethambutol.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:11919-11924(1996).
CC   -!- FUNCTION: Arabinosyl transferase responsible for the polymerization of
CC       arabinose into the arabinan of arabinogalactan.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the emb family. {ECO:0000305}.
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DR   EMBL; U66560; AAC44547.1; -; Genomic_DNA.
DR   AlphaFoldDB; P71485; -.
DR   SMR; P71485; -.
DR   CAZy; GT53; Glycosyltransferase Family 53.
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:0052636; F:arabinosyltransferase activity; IEA:InterPro.
DR   GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.610; -; 1.
DR   Gene3D; 2.60.120.940; -; 1.
DR   InterPro; IPR032731; Arabino_trans_C.
DR   InterPro; IPR042486; Arabino_trans_C_2.
DR   InterPro; IPR007680; Arabino_trans_central.
DR   InterPro; IPR040920; Arabino_trans_N.
DR   InterPro; IPR027451; EmbABC_dom1.
DR   Pfam; PF14896; Arabino_trans_C; 1.
DR   Pfam; PF17689; Arabino_trans_N; 1.
DR   Pfam; PF04602; Arabinose_trans; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Cell wall biogenesis/degradation;
KW   Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1108
FT                   /note="Probable arabinosyltransferase A"
FT                   /id="PRO_0000220560"
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        531..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        582..604
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        616..638
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        653..675
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        696..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          804..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1108 AA;  117405 MW;  0ED8E648768075FA CRC64;
     MPHDGKQRSQ RIPRSVAAVA GIAGLLLCLA VPLLPVRQTT ATVLWPQGTV DGHVSQITAP
     LVSGAPRALD ISIPCPAVAT LPADGGLVVS TLPPGGMDAG KNGLFVRANK DVVVVAFRDT
     VAAVAQRPAV AAGACSVLHA WADAGAAGAE FVGIPGAAGT LPAEKKPQVG GIFTDLKVPA
     GPGLSARVDI DTRFITAPTV LKQIVMVLGT LAVLTAIVAL AVLDRRSRGG GTLINWRSPI
     AWLSRYRPGT HLANWRRVGL ATWIADAAVL ATLLLWHVVG ATSSDDGYNL TIARVAPKAG
     YLVDYYRYFG TTDAPFDWYL GLLSRLASVS TAGVWMRLPA TLAGIGCWLI ISHWVLRRLG
     PGRGGLAANR VAVFTAGAVF VAAWLPFNNG LRPEPLIALG VLVTWMLVER AIALQRLAPA
     AVAVVVALLT ATLAPQGLIA VAALLTGARA VAQAIRRRRA SDGLLAPLAV LAAALSLILV
     VVFRSQTVAT VLESARIKYK VGPTIAWYQD WLRYYFLTVE SNPDGSMARR FAVLVMLLCL
     FGMLVILLRR GHVPGVASGP RWRLIGTTAV GLLLLTFTPT KWAVQFGAFA GLAGALGALT
     AFACSRIGLH NRRNLTLYVT ALLFVLAWAT SGINGWFYVG NYGVPWYDIQ PVIASHPVTS
     MFLTLSIITG LLAAWQHFRM DYAGHTEVKD SRRNRVLAST PLLVVATIMV VGEVASLTKG
     AVFRYPLYTT GKANLAAIAS GLSPTSCAMA DDVLAEPDAN AGMLQPLPGQ TFGPDGPLGG
     VNPVGFKPDG VGDDLQSDPV VTKPGLVNSD ASPNKPNVAY SDSAGTAGGK GPVGVNGSHA
     ALPFGLDPAR TPVMGSYGEN SLAATATSAW YQLPPRTPDR PLVVVSAAGA IWSYKEDGTF
     TYGQSLKLQW GVARPDGSTV PLAEVQPIDI GPQPAWRNLR FPLAWAPPEA NVARIVAYDP
     NLSSEQWFAF TPPRVPVTET LQQLIGSQTP VMMDIATAAN FPCQRPFSEH LGVAELPAYR
     ILPDRKQTAA SSNLWQSSEA GGPFLFLQAL LRTSTIPTYL RGDWYRDWGS VEQYFRLVPA
     DQAPDAAIEQ GVMTVHGWSR QGPIRALP