ID EMBB_MYCTU Reviewed; 1098 AA. AC P9WNL7; L0TDT8; P72030; P72061; DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 1. DT 02-DEC-2020, entry version 36. DE RecName: Full=Probable arabinosyltransferase B; DE EC=2.4.2.-; GN Name=embB; OrderedLocusNames=Rv3795; ORFNames=MTCY13D12.29; 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 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 [4] RP VARIANTS EMB RESISTANT LEU-306; ILE-306; VAL-306 AND VAL-330. RX PubMed=9257740; DOI=10.1128/aac.41.8.1677; RA Sreevatsan S., Stockbauer K.E., Pan X., Kreiswirth B.N., Moghazeh S.L., RA Jacobs W.R. Jr., Telenti A., Musser J.M.; RT "Ethambutol resistance in Mycobacterium tuberculosis: critical role of embB RT mutations."; RL Antimicrob. Agents Chemother. 41:1677-1681(1997). RN [5] RP VARIANTS EMB RESISTANT. 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). RN [6] RP VARIANTS EMB RESISTANT LEU-306; ILE-306 AND VAL-306. RX PubMed=11162078; DOI=10.1006/mcpr.2000.0339; RA Rinder H., Mieskes K.T., Tortoli E., Richter E., Casal M., Vaquero M., RA Cambau E., Feldmann K., Loescher T.; RT "Detection of embB codon 306 mutations in ethambutol resistant RT Mycobacterium tuberculosis directly from sputum samples: a low-cost, rapid RT approach."; RL Mol. Cell. Probes 15:37-42(2001). RN [7] 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). 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 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}. 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; U68480; AAC45281.1; -; Genomic_DNA. DR EMBL; AL123456; CCP46624.1; -; Genomic_DNA. DR PIR; G70697; G70697. DR RefSeq; NP_218312.1; NC_000962.3. DR RefSeq; WP_003901728.1; NZ_NVQJ01000009.1. DR PDB; 7BVF; EM; 2.97 A; B=1-1098. DR PDBsum; 7BVF; -. DR SMR; P9WNL7; -. DR STRING; 83332.Rv3795; -. DR DrugBank; DB00330; Ethambutol. DR CAZy; GT53; Glycosyltransferase Family 53. DR TCDB; 9.B.364.1.5; the putative arabinosyltransferase b (aratb) family. DR PaxDb; P9WNL7; -. DR EnsemblBacteria; CCP46624; CCP46624; Rv3795. DR GeneID; 23489916; -. DR GeneID; 886126; -. DR KEGG; mtu:Rv3795; -. DR KEGG; mtv:RVBD_3795; -. DR TubercuList; Rv3795; -. DR eggNOG; COG1807; Bacteria. DR OMA; TPDYNAK; -. DR PhylomeDB; P9WNL7; -. DR BioCyc; MetaCyc:G185E-8091-MONOMER; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005618; C:cell wall; HDA:MTBBASE. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE. 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 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..1098 FT /note="Probable arabinosyltransferase B" FT /id="PRO_0000220569" FT TRANSMEM 28..50 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 217..239 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 271..293 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 402..419 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 434..456 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 472..494 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 541..558 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 570..587 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 597..619 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 626..648 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 663..685 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 698..720 FT /note="Helical" FT /evidence="ECO:0000255" FT VARIANT 297 FT /note="S -> A (resistance to EMB)" FT VARIANT 306 FT /note="M -> I (resistance to EMB)" FT /evidence="ECO:0000269|PubMed:11162078, FT ECO:0000269|PubMed:9257740" FT VARIANT 306 FT /note="M -> L (resistance to EMB)" FT /evidence="ECO:0000269|PubMed:11162078, FT ECO:0000269|PubMed:9257740" FT VARIANT 306 FT /note="M -> V (resistance to EMB)" FT /evidence="ECO:0000269|PubMed:11162078, FT ECO:0000269|PubMed:9257740" FT VARIANT 328 FT /note="D -> G (resistance to EMB)" FT VARIANT 328 FT /note="D -> Y (resistance to EMB)" FT VARIANT 330 FT /note="F -> V (resistance to EMB)" FT /evidence="ECO:0000269|PubMed:9257740" FT VARIANT 334 FT /note="Y -> H (resistance to EMB)" FT VARIANT 406 FT /note="G -> A (resistance to EMB)" FT VARIANT 406 FT /note="G -> C (resistance to EMB)" FT VARIANT 406 FT /note="G -> D (resistance to EMB)" FT VARIANT 497 FT /note="Q -> K (resistance to EMB)" FT VARIANT 497 FT /note="Q -> R (resistance to EMB)" FT VARIANT 745 FT /note="G -> D (resistance to EMB)" FT VARIANT 959 FT /note="D -> A (resistance to EMB)" FT VARIANT 1000 FT /note="M -> R (resistance to EMB)" FT VARIANT 1024 FT /note="D -> N (resistance to EMB)" FT CONFLICT 773..774 FT /note="SW -> FL (in Ref. 1)" FT /evidence="ECO:0000305" FT HELIX 25..39 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 44..46 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 49..56 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 60..63 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 77..81 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 85..89 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 98..102 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 122..126 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 128..136 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 137..140 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 141..144 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 161..163 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 167..169 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 202..205 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 212..214 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 216..239 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 278..293 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 300..308 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 309..312 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 313..315 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 320..324 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 334..340 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 341..343 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 347..350 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 353..368 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 370..372 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 375..377 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 381..395 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 396..398 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 401..403 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 405..422 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 423..426 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 430..442 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 446..448 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 452..457 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 460..470 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 476..479 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 481..484 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 485..487 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 490..493 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 495..497 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 499..511 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 518..521 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 522..526 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 527..529 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 530..535 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 537..559 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 570..584 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 593..600 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 603..613 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 616..618 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 622..639 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 648..651 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 657..659 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 663..665 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 668..687 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 697..701 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 706..727 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 735..741 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 748..751 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 753..758 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 771..773 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 779..781 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 795..798 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 813..815 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 826..828 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 839..841 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 850..852 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 874..883 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 888..891 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 901..903 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 926..928 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 932..935 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 936..938 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 945..947 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 961..967 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 974..977 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 980..982 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 984..986 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 991..993 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 1002..1007 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 1011..1015 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 1018..1023 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 1025..1028 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 1031..1033 FT /evidence="ECO:0000244|PDB:7BVF" FT TURN 1037..1039 FT /evidence="ECO:0000244|PDB:7BVF" FT HELIX 1040..1043 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 1046..1048 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 1050..1055 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 1063..1067 FT /evidence="ECO:0000244|PDB:7BVF" FT STRAND 1080..1084 FT /evidence="ECO:0000244|PDB:7BVF" SQ SEQUENCE 1098 AA; 118021 MW; DD7D7025DC803833 CRC64; MTQCASRRKS TPNRAILGAF ASARGTRWVA TIAGLIGFVL SVATPLLPVV QTTAMLDWPQ RGQLGSVTAP LISLTPVDFT ATVPCDVVRA MPPAGGVVLG TAPKQGKDAN LQALFVVVSA QRVDVTDRNV VILSVPREQV TSPQCQRIEV TSTHAGTFAN FVGLKDPSGA PLRSGFPDPN LRPQIVGVFT DLTGPAPPGL AVSATIDTRF STRPTTLKLL AIIGAIVATV VALIALWRLD QLDGRGSIAQ LLLRPFRPAS SPGGMRRLIP ASWRTFTLTD AVVIFGFLLW HVIGANSSDD GYILGMARVA DHAGYMSNYF RWFGSPEDPF GWYYNLLALM THVSDASLWM RLPDLAAGLV CWLLLSREVL PRLGPAVEAS KPAYWAAAMV LLTAWMPFNN GLRPEGIIAL GSLVTYVLIE RSMRYSRLTP AALAVVTAAF TLGVQPTGLI AVAALVAGGR PMLRILVRRH RLVGTLPLVS PMLAAGTVIL TVVFADQTLS TVLEATRVRA KIGPSQAWYT ENLRYYYLIL PTVDGSLSRR FGFLITALCL FTAVFIMLRR KRIPSVARGP AWRLMGVIFG TMFFLMFTPT KWVHHFGLFA AVGAAMAALT TVLVSPSVLR WSRNRMAFLA ALFFLLALCW ATTNGWWYVS SYGVPFNSAM PKIDGITVST IFFALFAIAA GYAAWLHFAP RGAGEGRLIR ALTTAPVPIV AGFMAAVFVA SMVAGIVRQY PTYSNGWSNV RAFVGGCGLA DDVLVEPDTN AGFMKPLDGD SGSWGPLGPL GGVNPVGFTP NGVPEHTVAE AIVMKPNQPG TDYDWDAPTK LTSPGINGST VPLPYGLDPA RVPLAGTYTT GAQQQSTLVS AWYLLPKPDD GHPLVVVTAA GKIAGNSVLH GYTPGQTVVL EYAMPGPGAL VPAGRMVPDD LYGEQPKAWR NLRFARAKMP ADAVAVRVVA EDLSLTPEDW IAVTPPRVPD LRSLQEYVGS TQPVLLDWAV GLAFPCQQPM LHANGIAEIP KFRITPDYSA KKLDTDTWED GTNGGLLGIT DLLLRAHVMA TYLSRDWARD WGSLRKFDTL VDAPPAQLEL GTATRSGLWS PGKIRIGP //