EMBB_MYCSM
ID EMBB_MYCSM Reviewed; 1082 AA.
AC Q50395; O30406;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable arabinosyltransferase B;
DE EC=2.4.2.-;
GN Name=embB;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS EMB RESISTANT PHE-289;
RP MET-289 AND THR-292.
RC STRAIN=em30;
RX PubMed=9420031; DOI=10.1128/aac.41.12.2629;
RA Lety M.A., Nair S., Berche P., Escuyer V.;
RT "A single point mutation in the embB gene is responsible for resistance to
RT ethambutol in Mycobacterium smegmatis.";
RL Antimicrob. Agents Chemother. 41:2629-2633(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; AAC45273.1; -; Genomic_DNA.
DR EMBL; AF004289; AAB69157.1; -; Genomic_DNA.
DR PIR; T45096; T45096.
DR AlphaFoldDB; Q50395; -.
DR SMR; Q50395; -.
DR CAZy; GT53; Glycosyltransferase Family 53.
DR PRIDE; Q50395; -.
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..1082
FT /note="Probable arabinosyltransferase B"
FT /id="PRO_0000220568"
FT TRANSMEM 28..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 289
FT /note="I -> F (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:9420031"
FT VARIANT 289
FT /note="I -> M (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:9420031"
FT VARIANT 292
FT /note="M -> T (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:9420031"
FT CONFLICT 453
FT /note="I -> M (in Ref. 2; AAB69157)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="D -> V (in Ref. 2; AAB69157)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="K -> N (in Ref. 2; AAB69157)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="T -> I (in Ref. 2; AAB69157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1082 AA; 116777 MW; 10883EA54F72E0FE CRC64;
MSGNMDEAVS GNMDEAVSAG KDVRIARWVA TIAGLLGFVL SVSIPLLPVT QTTATLNWPQ
QGRLDNVTAP LISQAPLELT ATVPCSVVRD LPPEGGLVFG TAPAEGRDAA LNAMLVNVTE
TRVDVIVRNV VVASVNRDRV AGPDCQRIEI TSNLDGTYAD FVGLTQISGE DAGKLQRTGY
PDPNLRPAIV GVFTDLTGPA PQGLSVSAEI DTRFTTHPTA LKLAAMLLAI VSTVIALLAL
WRLDRLDGRR MHRLIPTRWR TVTAVDGVVV GGMAIWYVIG ANSSDDGYIL QMARTAEHAG
YMANYFRWFG SPEDPFGWYY NVLALMTKVS DASIWIRLPD LICALICWLL LSREVLPRLG
PAVAGSRAAM WAAGLVLLGA WMPFNNGLRP EGQIATGALI TYVLIERAVT SGRLTPAALA
ITTAAFTLGI QPTGLIAVAA LLAGGRPILR IVIRRRRLDG TWPLIAPLLA AGTVILAVVF
ADQTIATVLE ATRIRTAIGP SQEWWTEKLR YYYLILPTTD GAISRRVAFV FTAMCLFPSL
FMMLRRKHIA GVARGPAWRL MGIIFATMFF LMFTPTKWTH HFGLFAAVGG AMAALATVLV
SPTVLRSARN RMAFLSLVLF VLAFCFASTN GWWYVSNFGA PFNNSVPKVG GVQISAIFFA
LSAIAALWAF WLHLTRRTES RVVDRLTAAP IPVAAGFMVV VMMASMAIGV VRQYPTYSNG
WANIRAFAGG CGLADDVLVE PDSNAGFLTP LPGAYGPLGP LGGEDPQGFS PDGVPDRIIA
EAIRLNNPQP GTDYDWNRPI KLDEPGINGS TVPLPYGLDP KRVPVAGTYS TEAQQESRLS
SAWYELPARD ETERAAHPLV VITAAGTITG ESVANGLTTG QTVDLEYATR GPDGTLVPAG
RVTPYDVGPT PSWRNLRYPR SEIPDDAVAV RVVAEDLSLS QGDWIAVTPP RVPELQSVQE
YVGSDQPVLM DWAVGLAFPC QQPMLHANGV TEVPKFRISP DYYAKLQSTD TWQDGINGGL
LGITDLLLRA SVMSTYLSQD WGQDWGSLRK FDTVVEATPA ELDFGSQTHS GLYSPGPLRI
RP
