ID   EMBA_MYCTO              Reviewed;        1094 AA.
AC   P9WNL8; L0TDK4; P0A560; P72029; P72060;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Probable arabinosyltransferase A;
DE            EC=2.4.2.-;
GN   Name=embA; OrderedLocusNames=MT3901;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Arabinosyl transferase responsible for the polymerization of
CC       arabinose into the arabinan of arabinogalactan. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the emb family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48267.1; -; Genomic_DNA.
DR   PIR; F70697; F70697.
DR   RefSeq; WP_003899696.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNL8; -.
DR   SMR; P9WNL8; -.
DR   DrugCentral; P9WNL8; -.
DR   CAZy; GT53; Glycosyltransferase Family 53.
DR   EnsemblBacteria; AAK48267; AAK48267; MT3901.
DR   KEGG; mtc:MT3901; -.
DR   PATRIC; fig|83331.31.peg.4198; -.
DR   HOGENOM; CLU_010182_0_0_11; -.
DR   Proteomes; UP000001020; 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: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..1094
FT                   /note="Probable arabinosyltransferase A"
FT                   /id="PRO_0000427104"
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        519..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        543..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        575..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        604..626
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        641..663
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        684..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1094 AA;  115724 MW;  11EEA34999633EEC CRC64;
     MPHDGNERSH RIARLAAVVS GIAGLLLCGI VPLLPVNQTT ATIFWPQGST ADGNITQITA
     PLVSGAPRAL DISIPCSAIA TLPANGGLVL STLPAGGVDT GKAGLFVRAN QDTVVVAFRD
     SVAAVAARST IAAGGCSALH IWADTGGAGA DFMGIPGGAG TLPPEKKPQV GGIFTDLKVG
     AQPGLSARVD IDTRFITTPG ALKKAVMLLG VLAVLVAMVG LAALDRLSRG RTLRDWLTRY
     RPRVRVGFAS RLADAAVIAT LLLWHVIGAT SSDDGYLLTV ARVAPKAGYV ANYYRYFGTT
     EAPFDWYTSV LAQLAAVSTA GVWMRLPATL AGIACWLIVS RFVLRRLGPG PGGLASNRVA
     VFTAGAVFLS AWLPFNNGLR PEPLIALGVL VTWVLVERSI ALGRLAPAAV AIIVATLTAT
     LAPQGLIALA PLLTGARAIA QRIRRRRATD GLLAPLAVLA AALSLITVVV FRDQTLATVA
     ESARIKYKVG PTIAWYQDFL RYYFLTVESN VEGSMSRRFA VLVLLFCLFG VLFVLLRRGR
     VAGLASGPAW RLIGTTAVGL LLLTFTPTKW AVQFGAFAGL AGVLGAVTAF TFARIGLHSR
     RNLTLYVTAL LFVLAWATSG INGWFYVGNY GVPWYDIQPV IASHPVTSMF LTLSILTGLL
     AAWYHFRMDY AGHTEVKDNR RNRILASTPL LVVAVIMVAG EVGSMAKAAV FRYPLYTTAK
     ANLTALSTGL SSCAMADDVL AEPDPNAGML QPVPGQAFGP DGPLGGISPV GFKPEGVGED
     LKSDPVVSKP GLVNSDASPN KPNAAITDSA GTAGGKGPVG INGSHAALPF GLDPARTPVM
     GSYGENNLAA TATSAWYQLP PRSPDRPLVV VSAAGAIWSY KEDGDFIYGQ SLKLQWGVTG
     PDGRIQPLGQ VFPIDIGPQP AWRNLRFPLA WAPPEADVAR IVAYDPNLSP EQWFAFTPPR
     VPVLESLQRL IGSATPVLMD IATAANFPCQ RPFSEHLGIA ELPQYRILPD HKQTAASSNL
     WQSSSTGGPF LFTQALLRTS TIATYLRGDW YRDWGSVEQY HRLVPADQAP DAVVEEGVIT
     VPGWGRPGPI RALP