ID   EMBC_MYCSM              Reviewed;        1074 AA.
AC   Q50393;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Probable arabinosyltransferase C;
DE            EC=2.4.2.-;
GN   Name=embC;
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; AAC45271.1; -; Genomic_DNA.
DR   PIR; T45094; T45094.
DR   AlphaFoldDB; Q50393; -.
DR   SMR; Q50393; -.
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..1074
FT                   /note="Probable arabinosyltransferase C"
FT                   /id="PRO_0000220572"
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        452..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        516..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        573..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        608..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        645..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        684..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1074 AA;  115392 MW;  68DB19FE8839C301 CRC64;
     MTGPHAAGGS NHRTARLVAI IAGLLGTLMA IATPLLPVEQ TTAELNWPQN GVWQSVDAPL
     IGYVATDLTV TVPCQAAAGL VGPENRNRSV LLSTVPKQAP KAIDRGLLIE RINNDLTVIV
     RNTPVVSAPL EQVLSPDCRY LTFTAHADKV TGEFVGLTQG PDDDDPGEAV RGERSGYDFR
     PQIVGVFTDL SGPAPEGLQL SATIDTRYST SPTLLKLLAM IVGVAMTVIA LGALHVLDCA
     DGRRHKRFLP SRWWSMTPLD GLVSAMLVWW HFVGANTADD GYILTMARVS EHAGYMANYY
     RWFGTPESPF GWYYDLLALW AHVSTASVWM RFPTLLMGLA CWWVISREVI PRLGAAAKHS
     RAAAWTAAGL FLAFWLPLNN GLRPEPIIAL GILLTWCSVE RGVATSRLLP VAVAIIIGAL
     TLFSGPTGIA AVGALLVAIG PLKTIVAAHV SRFGYWALLA PIAAAGTVTI FLIFRDQTLA
     AELQASSFKS AVGPSLAWFD EHIRYSRLFT TSPDGSVARR FAVLTLLLAL AVSIAMTLRK
     GRIPGTALGP SRRIIGITII SFLAMMFTPT KWTHQFGVFA GLAGCLGALA AVAVTTTAMK
     SRRNRTVFGA AVLFVTALSF ATVNGWWYVS NFGVPWSNSF PEFKFGFTTM LLGLSVLALL
     VAAWFHFSGR DVSPDRPQRR WQRLLVAPLA VATWALVIFE VVSLTLGMIN QYPAWSVGRS
     NLNALTGKTC GLANDVLVEQ NANAGMLTPI GEPAGQALGA VTSLGFGPNG IPSDVSADPV
     MEQPGTDNFA DSDSGVVTGT EVGTEGGTTA AAGINGSRAR LPYGLNPATT PVLGSWRSGT
     QQPAVLRSAW YRLPDRDQAG PLLVVSAAGR FDQGEVEVQW ATDEQAAANE PGGSITFGDV
     GAAPAWRNLR APLSSIPPEA TQIRLVASDD DLAPQHWIAL TPPRIPELRT LQEVVGSSDP
     VMLDWLVGLA FPCQRPFDHR YGVVEVPKWR ILPDRFGAEA NSPVMDYLGG GPLGITELLL
     RPSSVPTYLK DDWYRDWGSL QRLTPWYPDA QPARLDLGTA TRSGWWSPAP LRLS