ID   EMBB_MYCAV              Reviewed;        1065 AA.
AC   P71486;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 87.
DE   RecName: Full=Probable arabinosyltransferase B;
DE            EC=2.4.2.-;
GN   Name=embB;
OS   Mycobacterium avium.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U66560; AAC44548.1; -; Genomic_DNA.
DR   AlphaFoldDB; P71486; -.
DR   SMR; P71486; -.
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   FunFam; 2.60.120.940:FF:000001; Membrane indolylacetylinositol arabinosyltransferase embC; 1.
DR   Gene3D; 3.40.190.160; -; 1.
DR   Gene3D; 2.60.120.610; arabinofuranosyltransferase like domain; 1.
DR   Gene3D; 2.60.120.940; EmbC, C-terminal domain, subdomain 2; 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..1065
FT                   /note="Probable arabinosyltransferase B"
FT                   /id="PRO_0000220565"
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        510..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        540..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        567..589
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        596..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        633..655
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        667..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1065 AA;  114625 MW;  3F12D113678C62BF CRC64;
     MSVSTVGGDV RVTRWVATIA GLIGFVLSVA TPLLPVVQTT ATLNWPQGGQ LNSVTAPLIS
     LTPVDLTATV PCSLVRDLPP GGGVILSTGP KKGKDAALNA LFVVAHGKRV DVTDRNVVIA
     SASRDQVAGA GCSRIEIAST RAGTFATFVG LTDPAGKPLG GGFPDPNLRP QIVGVFTDLT
     GPAPAGLKLS ATIDTRFSTT PTTLKLAAMV TAILATIVAL VALWRLDQLD GHRMRRLIPA
     NWRTFTLADV AVIFGFVLWH VIGANSSDDG YILGMARVAD RAGYMSNYFR WFGSPEDPFG
     WYYNLLALMT HVSDASLWMR LPDLFAGIVC WLLLSREVLP RLGPAVAASR PANWAAGMVL
     LTAWMPFDNG LRPEPIIALG SLVTYVLIER SMRYSRLTPA ALAVITAAFT LGVQPTGLIA
     VAALVAGGRP ILRILVRRHR VVGTWPLVAP MLAAGTVILT VVFADQTLAT VLEATRIRTA
     IGPSQAWYTE NLRYYYLILP TVDGSLSRRF GFLITALCLF TAVFIMLRRK RIPGVARGPA
     WRLMGVIFGT MFFLMFTPTK WVHHFGLFAA VGAAMAALTT VLVSPAVLGW SRNRMAFLAA
     LLFMMALCFA TTNGWWYVSS YGVPFNSTMP KIGGITVSTV FFSMFVAAAL YAIWLHFASR
     EHGEGRLARA LTAAPVPLAA GFMALVFIAS MVAGIVRQYP TYSNAWDNLR EFSGGCGLAD
     DVLVEPDSNV GYMTPLGGDY GPLGPLGGQH PVGFSPNGVP EHTVAEAIRI TPNQPGTDYD
     WDAPTKLSAP GINGSTVPLP YGLDAARVPL AGSYTTGAQQ QSRLTSAWYR LPAPDDGHPL
     VVVTAAGKIA GNSVLHHHTD GQTVVLEYGR PGPGGDIVPA GRLVPYDLYG EQPKAWRNLR
     FARSDMPADT VAVRVVAEDL SLTPEDWIAV TPPRVPEMRS LQEYVGSTQP VLMDWAVGLA
     FPCQQPMLHV NGVTEIPKFR ITPDYTAKKM DTDTWEDGTN GGLLGITDLL LRAHVMSTYL
     SHDWGRDWGS LRRFETIADA HPAQLDLGTA TRTGWWSPGP IRIKP
//