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P9WNL7 (EMBB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 1. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable arabinosyltransferase B

EC=2.4.2.-
Gene names
Name:embB
Ordered Locus Names:Rv3795
ORF Names:MTCY13D12.29
OrganismMycobacterium tuberculosis (strain ATCC 25618 / H37Rv) [Reference proteome] [HAMAP]
Taxonomic identifier83332 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length1098 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.

Subcellular location

Cell membrane; Multi-pass membrane protein Probable.

Induction

Positively regulated by the transcriptional regulatory protein EmbR. Ref.6

Miscellaneous

This is one of the targets of the anti-tuberculosis drug ethambutol [(S,S')-2,2'-(ethylenediimino)di-1-butanol; EMB]. EMB is a first-line drug used to treat tuberculosis. EMB inhibits the transfer of arabinogalactan into the cell wall.

Sequence similarities

Belongs to the emb family.

Ontologies

Keywords
   Biological processAntibiotic resistance
Cell wall biogenesis/degradation
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10981098Probable arabinosyltransferase B
PRO_0000220569

Regions

Transmembrane28 – 5023Helical; Potential
Transmembrane217 – 23923Helical; Potential
Transmembrane271 – 29323Helical; Potential
Transmembrane402 – 41918Helical; Potential
Transmembrane434 – 45623Helical; Potential
Transmembrane472 – 49423Helical; Potential
Transmembrane541 – 55818Helical; Potential
Transmembrane570 – 58718Helical; Potential
Transmembrane597 – 61923Helical; Potential
Transmembrane626 – 64823Helical; Potential
Transmembrane663 – 68523Helical; Potential
Transmembrane698 – 72023Helical; Potential

Natural variations

Natural variant2971S → A Resistance to EMB.
Natural variant3061M → I Resistance to EMB. Ref.3 Ref.5
Natural variant3061M → L Resistance to EMB. Ref.3 Ref.5
Natural variant3061M → V Resistance to EMB. Ref.3 Ref.5
Natural variant3281D → G Resistance to EMB.
Natural variant3281D → Y Resistance to EMB.
Natural variant3301F → V Resistance to EMB. Ref.3
Natural variant3341Y → H Resistance to EMB.
Natural variant4061G → A Resistance to EMB.
Natural variant4061G → C Resistance to EMB.
Natural variant4061G → D Resistance to EMB.
Natural variant4971Q → K Resistance to EMB.
Natural variant4971Q → R Resistance to EMB.
Natural variant7451G → D Resistance to EMB.
Natural variant9591D → A Resistance to EMB.
Natural variant10001M → R Resistance to EMB.
Natural variant10241D → N Resistance to EMB.

Experimental info

Sequence conflict773 – 7742SW → FL Ref.1

Sequences

Sequence LengthMass (Da)Tools
P9WNL7 [UniParc].

Last modified April 16, 2014. Version 1.
Checksum: DD7D7025DC803833

FASTA1,098118,021
        10         20         30         40         50         60 
MTQCASRRKS TPNRAILGAF ASARGTRWVA TIAGLIGFVL SVATPLLPVV QTTAMLDWPQ 

        70         80         90        100        110        120 
RGQLGSVTAP LISLTPVDFT ATVPCDVVRA MPPAGGVVLG TAPKQGKDAN LQALFVVVSA 

       130        140        150        160        170        180 
QRVDVTDRNV VILSVPREQV TSPQCQRIEV TSTHAGTFAN FVGLKDPSGA PLRSGFPDPN 

       190        200        210        220        230        240 
LRPQIVGVFT DLTGPAPPGL AVSATIDTRF STRPTTLKLL AIIGAIVATV VALIALWRLD 

       250        260        270        280        290        300 
QLDGRGSIAQ LLLRPFRPAS SPGGMRRLIP ASWRTFTLTD AVVIFGFLLW HVIGANSSDD 

       310        320        330        340        350        360 
GYILGMARVA DHAGYMSNYF RWFGSPEDPF GWYYNLLALM THVSDASLWM RLPDLAAGLV 

       370        380        390        400        410        420 
CWLLLSREVL PRLGPAVEAS KPAYWAAAMV LLTAWMPFNN GLRPEGIIAL GSLVTYVLIE 

       430        440        450        460        470        480 
RSMRYSRLTP AALAVVTAAF TLGVQPTGLI AVAALVAGGR PMLRILVRRH RLVGTLPLVS 

       490        500        510        520        530        540 
PMLAAGTVIL TVVFADQTLS TVLEATRVRA KIGPSQAWYT ENLRYYYLIL PTVDGSLSRR 

       550        560        570        580        590        600 
FGFLITALCL FTAVFIMLRR KRIPSVARGP AWRLMGVIFG TMFFLMFTPT KWVHHFGLFA 

       610        620        630        640        650        660 
AVGAAMAALT TVLVSPSVLR WSRNRMAFLA ALFFLLALCW ATTNGWWYVS SYGVPFNSAM 

       670        680        690        700        710        720 
PKIDGITVST IFFALFAIAA GYAAWLHFAP RGAGEGRLIR ALTTAPVPIV AGFMAAVFVA 

       730        740        750        760        770        780 
SMVAGIVRQY PTYSNGWSNV RAFVGGCGLA DDVLVEPDTN AGFMKPLDGD SGSWGPLGPL 

       790        800        810        820        830        840 
GGVNPVGFTP NGVPEHTVAE AIVMKPNQPG TDYDWDAPTK LTSPGINGST VPLPYGLDPA 

       850        860        870        880        890        900 
RVPLAGTYTT GAQQQSTLVS AWYLLPKPDD GHPLVVVTAA GKIAGNSVLH GYTPGQTVVL 

       910        920        930        940        950        960 
EYAMPGPGAL VPAGRMVPDD LYGEQPKAWR NLRFARAKMP ADAVAVRVVA EDLSLTPEDW 

       970        980        990       1000       1010       1020 
IAVTPPRVPD LRSLQEYVGS TQPVLLDWAV GLAFPCQQPM LHANGIAEIP KFRITPDYSA 

      1030       1040       1050       1060       1070       1080 
KKLDTDTWED GTNGGLLGIT DLLLRAHVMA TYLSRDWARD WGSLRKFDTL VDAPPAQLEL 

      1090 
GTATRSGLWS PGKIRIGP 

« Hide

References

« Hide 'large scale' references
[1]"The emb operon, a gene cluster of Mycobacterium tuberculosis involved in resistance to ethambutol."
Telenti A., Philipp W.J., Sreevatsan S., Bernasconi C., Stockbauer K.E., Wieles B., Musser J.M., Jacobs W.R. Jr.
Nat. Med. 3:567-570(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[3]"Ethambutol resistance in Mycobacterium tuberculosis: critical role of embB mutations."
Sreevatsan S., Stockbauer K.E., Pan X., Kreiswirth B.N., Moghazeh S.L., Jacobs W.R. Jr., Telenti A., Musser J.M.
Antimicrob. Agents Chemother. 41:1677-1681(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EMB RESISTANT LEU-306; ILE-306; VAL-306 AND VAL-330.
[4]"Molecular genetic analysis of nucleotide polymorphisms associated with ethambutol resistance in human isolates of Mycobacterium tuberculosis."
Ramaswamy S.V., Amin A.G., Goeksel S., Stager C.E., Dou S.-J., El Sahly H., Moghazeh S.L., Kreiswirth B.N., Musser J.M.
Antimicrob. Agents Chemother. 44:326-336(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EMB RESISTANT.
[5]"Detection of embB codon 306 mutations in ethambutol resistant Mycobacterium tuberculosis directly from sputum samples: a low-cost, rapid approach."
Rinder H., Mieskes K.T., Tortoli E., Richter E., Casal M., Vaquero M., Cambau E., Feldmann K., Loescher T.
Mol. Cell. Probes 15:37-42(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EMB RESISTANT LEU-306; ILE-306 AND VAL-306.
[6]"Transcriptional control of the mycobacterial embCAB operon by PknH through a regulatory protein, EmbR, in vivo."
Sharma K., Gupta M., Pathak M., Gupta N., Koul A., Sarangi S., Baweja R., Singh Y.
J. Bacteriol. 188:2936-2944(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U68480 Genomic DNA. Translation: AAC45281.1.
AL123456 Genomic DNA. Translation: CCP46624.1.
PIRG70697.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

TubercuListRv3795.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameEMBB_MYCTU
AccessionPrimary (citable) accession number: P9WNL7
Secondary accession number(s): L0TDT8, P72030, P72061
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: April 16, 2014
This is version 1 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families