Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9KWU7 (RPOB_THEAQ)

Last modified February 9, 2010. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    DNA-directed RNA polymerase subunit beta
      Short name=RNAP subunit beta
    EC=2.7.7.6
Alternative name(s):
    Transcriptase subunit beta
    RNA polymerase subunit beta
Gene names
Name: rpoB
OrganismThermus aquaticus
Taxonomic identifier271 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Hide | Top

Protein attributes

Sequence length1119 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. HAMAP MF_01321

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). HAMAP MF_01321

Subunit structure

The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. HAMAP MF_01321

Sequence similarities

Belongs to the RNA polymerase beta chain family.

Hide | Top

Ontologies

Keywords
   Biological processTranscription
   Cellular componentDNA-directed RNA polymerase
   Molecular functionNucleotidyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processtranscription, DNA-dependent

Inferred from electronic annotation. Source: HAMAP

   Molecular functionDNA binding

Inferred from electronic annotation. Source: HAMAP

DNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: HAMAP

ribonucleoside binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11191119DNA-directed RNA polymerase subunit beta HAMAP MF_01321
PRO_0000047983

Secondary structure

1 ................................................................................................................................................................................................ 1119
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9KWU7-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2CEF66FA79C77F33

FASTA1,119124,758
        10         20         30         40         50         60 
MEIKRFGRIR EVIPLPPLTE IQVESYKKAL QADVPPEKRE NVGIQAAFKE TFPIEEGDKG 

        70         80         90        100        110        120 
KGGLVLDFLE YRIGDPPFSQ DECREKDLTY QAPLYARLQL IHKDTGLIKE DEVFLGHLPL 

       130        140        150        160        170        180 
MTEDGSFIIN GADRVIVSQI HRSPGVYFTP DPARPGRYIA SIIPLPKRGP WIDLEVEASG 

       190        200        210        220        230        240 
VVTMKVNKRK FPLVLLLRVL GYDQETLVRE LSAYGDLVQG LLDEAVLAMR PEEAMVRLFT 

       250        260        270        280        290        300 
LLRPGDPPKK DKALAYLFGL LADPKRYDLG EAGRYKAEEK LGVGLSGRTL VRFEDGEFKD 

       310        320        330        340        350        360 
EVFLPTLRYL FALTAGVPGH EVDDIDHLGN RRIRTVGELM ADQFRVGLAR LARGVRERMV 

       370        380        390        400        410        420 
MGSPDTLTPA KLVNSRPLEA ALREFFSRSQ LSQFKDETNP LSSLRHKRRI SALGPGGLTR 

       430        440        450        460        470        480 
ERAGFDVRDV HRTHYGRICP VETPEGANIG LITSLAAYAR VDALGFIRTP YRRVKNGVVT 

       490        500        510        520        530        540 
EEVVYMTASE EDRYTIAQAN TPLEGDRIAT DRVVARRRGE PVIVAPEEVE FMDVSPKQVF 

       550        560        570        580        590        600 
SLNTNLIPFL EHDDANRALM GSNMQTQAVP LIRAQAPVVM TGLEERVVRD SLAALYAEED 

       610        620        630        640        650        660 
GEVVKVDGTR IAVRYEDGRL VEHPLRRYAR SNQGTAFDQR PRVRVGQRVK KGDLLADGPA 

       670        680        690        700        710        720 
SEEGFLALGQ NVLVAIMPFD GYNFEDAIVI SEELLKRDFY TSIHIERYEI EARDTKLGPE 

       730        740        750        760        770        780 
RITRDIPHLS EAALRDLDEE GIVRIGAEVK PGDILVGRTS FKGEQEPSPE ERLLRSIFGE 

       790        800        810        820        830        840 
KARDVKDTSL RVPPGEGGIV VGRLRLRRGD PGVELKPGVR EVVRVFVAQK RKLQVGDKLA 

       850        860        870        880        890        900 
NRHGNKGVVA KILPVEDMPH LPDGTPVDVI LNPLGVPSRM NLGQILETHL GLAGYFLGQR 

       910        920        930        940        950        960 
YISPVFDGAT EPEIKELLAE AFNLYFGKRQ GEGFGVDKRE KEVLARAEKL GLVSPGKSPE 

       970        980        990       1000       1010       1020 
EQLKELFDLG KVVLYDGRTG EPFEGPIVVG QMFIMKLYHM VEDKMHARST GPYSLITQQP 

      1030       1040       1050       1060       1070       1080 
LGGKAQFGGQ RFGEMEVWAL EAYGAAHTLQ EMLTIKSDDI EGRNAAYQAI IKGEDVPEPS 

      1090       1100       1110 
VPESFRVLVK ELQALALDVQ TLDEKDNPVD IFEGLASKR

« Hide

Hide | Top

References

[1]"Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution."
Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., Darst S.A.
Cell 98:811-824(1999) [PubMed: 10499798] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y19223 Genomic DNA. Translation: CAB65465.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HQMX-ray3.30C3-1119[»]
1I6VX-ray3.30C3-1119[»]
1L9UX-ray4.00C/L1-1119[»]
1L9ZX-ray6.50C1-1119[»]
1YNJX-ray3.20C1-1119[»]
1YNNX-ray3.30C1-1119[»]
2GHOX-ray5.00C1-1119[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.7.6. 118.

Family and domain databases

HAMAPMF_01321. RNApol_bact_RpoB.
[Tree]
InterProIPR010243. DNA-dir_RNA_pol_bsu_bac-type.
IPR019462. DNA-dir_RNA_pol_bsu_external_1.
IPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007641. RNA_pol_Rpb2_7.
[Graphical view]
PANTHERPTHR20856. RNA_pol_I_sub2. 1 hit.
PfamPF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 1 hit.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF10385. RNA_pol_Rpb2_45. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
TIGRFAMsTIGR02013. rpoB. 1 hit.
PROSITEPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameRPOB_THEAQ
AccessionPrimary (citable) accession number: Q9KWU7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents