EMBA_MYCTU
ID EMBA_MYCTU Reviewed; 1094 AA.
AC P9WNL9; L0TDK4; P0A560; P72029; P72060;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Probable arabinosyltransferase A;
DE EC=2.4.2.-;
GN Name=embA; OrderedLocusNames=Rv3794; ORFNames=MTCY13D12.28;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP INDUCTION.
RX PubMed=16585755; DOI=10.1128/jb.188.8.2936-2944.2006;
RA Sharma K., Gupta M., Pathak M., Gupta N., Koul A., Sarangi S., Baweja R.,
RA Singh Y.;
RT "Transcriptional control of the mycobacterial embCAB operon by PknH through
RT a regulatory protein, EmbR, in vivo.";
RL J. Bacteriol. 188:2936-2944(2006).
RN [4]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP VARIANTS EMB RESISTANT THR-201; SER-321; ASP-350; VAL-462; ALA-833 AND
RP SER-913.
RX PubMed=10639358; DOI=10.1128/aac.44.2.326-336.2000;
RA Ramaswamy S.V., Amin A.G., Goeksel S., Stager C.E., Dou S.-J., El Sahly H.,
RA Moghazeh S.L., Kreiswirth B.N., Musser J.M.;
RT "Molecular genetic analysis of nucleotide polymorphisms associated with
RT ethambutol resistance in human isolates of Mycobacterium tuberculosis.";
RL Antimicrob. Agents Chemother. 44:326-336(2000).
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 -!- INDUCTION: Positively regulated by the transcriptional regulatory
CC protein EmbR. {ECO:0000269|PubMed:16585755}.
CC -!- MISCELLANEOUS: This is one of the target 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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the emb family. {ECO:0000305}.
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DR EMBL; U68480; AAC45280.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46623.1; -; Genomic_DNA.
DR PIR; F70697; F70697.
DR RefSeq; NP_218311.1; NC_000962.3.
DR RefSeq; WP_003899696.1; NZ_NVQJ01000009.1.
DR PDB; 7BVF; EM; 2.97 A; A=2-1094.
DR PDBsum; 7BVF; -.
DR AlphaFoldDB; P9WNL9; -.
DR SMR; P9WNL9; -.
DR STRING; 83332.Rv3794; -.
DR BindingDB; P9WNL9; -.
DR ChEMBL; CHEMBL1877; -.
DR DrugBank; DB00330; Ethambutol.
DR DrugCentral; P9WNL9; -.
DR TCDB; 9.B.364.1.5; the putative arabinosyltransferase b (aratb) family.
DR PaxDb; P9WNL9; -.
DR GeneID; 886123; -.
DR KEGG; mtu:Rv3794; -.
DR TubercuList; Rv3794; -.
DR eggNOG; COG1807; Bacteria.
DR OMA; GWLHFRM; -.
DR PhylomeDB; P9WNL9; -.
DR BioCyc; MetaCyc:G185E-8090-MON; -.
DR PRO; PR:P9WNL9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0052636; F:arabinosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IMP:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell membrane;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1094
FT /note="Probable arabinosyltransferase A"
FT /id="PRO_0000220564"
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"
FT VARIANT 201
FT /note="A -> T (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:10639358"
FT VARIANT 321
FT /note="G -> S (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:10639358"
FT VARIANT 350
FT /note="G -> D (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:10639358"
FT VARIANT 462
FT /note="A -> V (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:10639358"
FT VARIANT 833
FT /note="D -> A (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:10639358"
FT VARIANT 913
FT /note="P -> S (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:10639358"
FT CONFLICT 116
FT /note="Missing (in Ref. 1; AAC45280)"
FT /evidence="ECO:0000305"
FT CONFLICT 899..900
FT /note="TG -> HR (in Ref. 1; AAC45280)"
FT /evidence="ECO:0000305"
FT HELIX 11..27
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 206..228
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 327..346
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 359..372
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 382..402
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 406..418
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 437..445
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 454..461
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 498..501
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 518..536
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 546..562
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 572..577
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 578..594
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 601..617
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 646..667
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 683..685
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 690..711
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 718..726
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 734..743
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 763..765
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 799..801
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 834..836
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 850..853
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 868..873
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 882..884
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 895..899
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 905..908
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 919..921
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 923..928
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 942..945
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 967..970
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 973..979
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 982..984
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 989..992
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1004..1008
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 1011..1016
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 1018..1021
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 1024..1027
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 1029..1031
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 1032..1035
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1036..1039
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1042..1046
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1056..1064
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 1066..1068
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1079..1081
FT /evidence="ECO:0007829|PDB:7BVF"
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
