ID   EMBA_MYCSM              Reviewed;        1092 AA.
AC   Q50394;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Probable arabinosyltransferase A;
DE            EC=2.4.2.-;
GN   Name=embA;
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=imm30;
RX   PubMed=9142129; DOI=10.1038/nm0597-567;
RA   Telenti A., Philipp W.J., Sreevatsan S., Bernasconi C., Stockbauer K.E.,
RA   Wieles B., Musser J.M., Jacobs W.R. Jr.;
RT   "The emb operon, a gene cluster of Mycobacterium tuberculosis involved in
RT   resistance to ethambutol.";
RL   Nat. Med. 3:567-570(1997).
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   -!- MISCELLANEOUS: This is one of the targets of the anti-tuberculosis drug
CC       ethambutol [(S,S')-2,2'-(ethylenediimino)di-1-butanol; EMB]. EMB is a
CC       first-line drug used to treat tuberculosis. EMB inhibits the transfer
CC       of arabinogalactan into the cell wall.
CC   -!- SIMILARITY: Belongs to the emb family. {ECO:0000305}.
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DR   EMBL; U46844; AAC45272.1; -; Genomic_DNA.
DR   PIR; T45095; T45095.
DR   AlphaFoldDB; Q50394; -.
DR   SMR; Q50394; -.
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..1092
FT                   /note="Probable arabinosyltransferase A"
FT                   /id="PRO_0000220563"
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        517..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        541..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        568..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        602..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        639..661
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        682..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          772..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1092 AA;  117055 MW;  62399B9F9EB24F3A CRC64;
     MPGDEQRERT ADDAVTEPSR IARLIAVVAG IAGVLLCGLV PLLPVEETTA TVLWPQGVGA
     DGNVTELTAP LVAGAPRALD VTIPCRAVAE LPADGGVVFS TNPAGGIEAG RNGMFIRANA
     DVVYVAFRDT VAAVAPREAV DSGACSEIHV WADVSAVGAD FAGIPDASGT LPVDKRPQVS
     GVFTDLKVPA QPGLAARIDI DTRFITSPTL LKTAVMVLGL ACVIGSIVAL ALLDRGWRRR
     PARTRGRAGL WTWITDTGVI GGLLIWHIVG APTSDDGYNM TIARVASEAG YTTNYYRYFG
     ASEAPFDWYQ SVLSHLASIS TAGVWMRLPA TAAAIATWLI ISRCVLPRIG RRVAANRVAM
     LTAGATFLAA WLPFNNGLRP EPLIAFAVIT VWMLVENSIG TRRLWPAAVA IVIAMFSVTL
     APQGLIALAP LLVGARAIGR VVTARRAAPG SWRPCPLAAS VAVVFVIIFR DQTLATVAES
     VRIKYVVGPT IPWYQEFLRY YFLTVEDSVD GSLTRRFAVL VLLLCLFGLI MVLLRRGRVP
     GAVSGPLWRL CGSTAIGLLL LILTPTKWAI QFGAFAGLAG ALGGVTAFAF ARVGLHSRRN
     LALYVTALLF ILAWATSGLN GWFYVGNYGV PWFDKQPVIA HYPVTTIFLV LAIVGGLLAG
     WLHFRMDYAG HTEVADTGRN RALASTPLLI VATIMVVLEL GSMVKATVGR YPVYTVGSAN
     IAALRSAGDS CAMADAVLVE ADPNEGMLQP VPGQRFGDYG PLGGEDPVGF TPSGVSEHLE
     PEPVGTNPGT PNSEGPVDKP NIGIAYAGDT GGGYAPEGVN GSRVFLPFGL DPSRTPVMGS
     YGENKLAAKA TSAWYQLPPR TPDRPLVTVA AAGAIWYYEE DGSFNYGQSL KLQWGVHRPD
     GTYQALSEVQ PIDIFQQKAW RNLRFPLAWA PPEANVARIV ADDPNLSEDQ WCAFTPPRVP
     VLQTAQQFLG SQTPVLMDIA TAANFPCQRP FAERLGVAEL PEYRIIPNFK QMVVSSNQWQ
     SAADGGPFLF IQALLRTEAI PTYLRDDWYR DWGSIERYIR VVPQEQAPTA AIEEGSTRVF
     GWSRGGPIRA LP