Probable arabinosyltransferase B - Mycobacterium tuberculosis

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P72030 (EMBB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Probable arabinosyltransferase B
EC=2.4.2.-

Gene names

Name:	embB
Ordered Locus Names:	Rv3795, MT3902
ORF Names:	MTCY13D12.29

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	1098 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7
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 process	Antibiotic resistance Cell wall biogenesis/degradation
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Actinobacterium-type cell wall biogenesis Inferred from electronic annotation. Source: InterPro growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell wall Inferred from direct assay PubMed 15525680. Source: MTBBASE integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay PubMed 15525680. Source: MTBBASE
Molecular_function	arabinosyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1098

1098

Probable arabinosyltransferase B

PRO_0000220569

Regions

Transmembrane

28 – 50

Helical; Potential

Transmembrane

217 – 239

Helical; Potential

Transmembrane

271 – 293

Helical; Potential

Transmembrane

402 – 419

Helical; Potential

Transmembrane

434 – 456

Helical; Potential

Transmembrane

472 – 494

Helical; Potential

Transmembrane

541 – 558

Helical; Potential

Transmembrane

570 – 587

Helical; Potential

Transmembrane

597 – 619

Helical; Potential

Transmembrane

626 – 648

Helical; Potential

Transmembrane

663 – 685

Helical; Potential

Transmembrane

698 – 720

Helical; Potential

Natural variations

Natural variant

297

S → A Resistance to EMB.

Natural variant

306

M → I Resistance to EMB. Ref.4 Ref.6

Natural variant

306

M → L Resistance to EMB. Ref.4 Ref.6

Natural variant

306

M → V Resistance to EMB. Ref.4 Ref.6

Natural variant

328

D → G Resistance to EMB.

Natural variant

328

D → Y Resistance to EMB.

Natural variant

330

F → V Resistance to EMB. Ref.4

Natural variant

334

Y → H Resistance to EMB.

Natural variant

406

G → A Resistance to EMB.

Natural variant

406

G → C Resistance to EMB.

Natural variant

406

G → D Resistance to EMB.

Natural variant

497

Q → K Resistance to EMB.

Natural variant

497

Q → R Resistance to EMB.

Natural variant

745

G → D Resistance to EMB.

Natural variant

959

D → A Resistance to EMB.

Natural variant

1000

M → R Resistance to EMB.

Natural variant

1024

D → N Resistance to EMB.

Experimental info

Sequence conflict

773 – 774

SW → FL Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P72030 [UniParc].

Last modified July 1, 1997. Version 2.
Checksum: DD7D7025DC803833
Show »

FASTA

1,098

118,021

        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' referencesShow '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. 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]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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	BX842584 Genomic DNA. Translation: CAB02474.1. U68480 Genomic DNA. Translation: AAC45281.1. AE000516 Genomic DNA. Translation: AAK48268.1. AL123456 Genomic DNA. Translation: CCP46624.1.
PIR	G70697.
RefSeq	NP_218312.1. NC_000962.3. NP_338454.1. NC_002755.2. YP_006517292.1. NC_018143.1.
3D structure databases
ProteinModelPortal	P72030.
SMR	P72030. Positions 56-200, 734-1067.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv3795.
Protein family/group databases
CAZy	GT53. Glycosyltransferase Family 53.
Proteomic databases
PRIDE	P72030.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK48268; AAK48268; MT3902.
GeneID	13317419. 886126. 926343.
KEGG	mtc:MT3902. mtu:Rv3795. mtv:RVBD_3795.
PATRIC	18130341. VBIMycTub22151_4258.
Organism-specific databases
TubercuList	Rv3795.
Phylogenomic databases
eggNOG	NOG04168.
HOGENOM	HOG000054334.
KO	K11386.
OMA	THHFGAY.
ProtClustDB	CLSK2748679.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-15270.
Family and domain databases
InterPro	IPR007680. Mycobac_arabinan_synth. [Graphical view]
Pfam	PF04602. Arabinose_trans. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00330. Ethambutol.

Entry information

Entry name

EMBB_MYCTU

Accession

Primary (citable) accession number: P72030
Secondary accession number(s): L0TDT8, P72061

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents