EMBB_MYCTU
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 03-AUG-2022, entry version 42.
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}.
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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 AlphaFoldDB; P9WNL7; -.
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 GeneID; 886126; -.
DR KEGG; mtu:Rv3795; -.
DR TubercuList; Rv3795; -.
DR eggNOG; COG1807; Bacteria.
DR OMA; TPDYNAK; -.
DR PhylomeDB; P9WNL7; -.
DR BioCyc; MetaCyc:G185E-8091-MON; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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:0007829|PDB:7BVF"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 216..239
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 300..308
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 353..368
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 381..395
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 405..422
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 430..442
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 452..457
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 460..470
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 485..487
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 499..511
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 522..526
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 537..559
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 570..584
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 593..600
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 603..613
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 622..639
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 648..651
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 668..687
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 697..701
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 706..727
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 735..741
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 748..751
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 753..758
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 771..773
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 779..781
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 795..798
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 813..815
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 839..841
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 850..852
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 874..883
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 888..891
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 926..928
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 932..935
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 936..938
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 945..947
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 961..967
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 974..977
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 980..982
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 984..986
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 991..993
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1002..1007
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1011..1015
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 1018..1023
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 1025..1028
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 1031..1033
FT /evidence="ECO:0007829|PDB:7BVF"
FT TURN 1037..1039
FT /evidence="ECO:0007829|PDB:7BVF"
FT HELIX 1040..1043
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1046..1048
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1050..1055
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1063..1067
FT /evidence="ECO:0007829|PDB:7BVF"
FT STRAND 1080..1084
FT /evidence="ECO:0007829|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
