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Protein

DNA-directed RNA polymerase subunit beta

Gene

rpoB

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit often mutates to generate rifampicin (Rif) resistance. Interaction with RbpA partially restores Rif-inhibited transcription; once the subunit is Rif-resistant however RbpA no longer stimulates transcription.UniRule annotation1 Publication

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance, Transcription

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-1367-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase subunit betaUniRule annotation (EC:2.7.7.6UniRule annotation)
Short name:
RNAP subunit betaUniRule annotation
Alternative name(s):
RNA polymerase subunit betaUniRule annotation
Transcriptase subunit betaUniRule annotation
Gene namesi
Name:rpoBUniRule annotation
Ordered Locus Names:MSMEG_1367, MSMEI_1328
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

Subcellular locationi

Keywords - Cellular componenti

DNA-directed RNA polymerase

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi429 – 4291Q → K or L: Rifampicin (Rif) resistant. 1 Publication
Mutagenesisi432 – 4321D → V: Rifampicin (Rif) resistant. 2 Publications
Mutagenesisi432 – 4321D → Y: Rifampicin (Rif) resistant; RbpA no longer rescues transcription in the presence of Rif. Decreased affinity for Rif, no change in affinity for RbpA. 2 Publications
Mutagenesisi442 – 4421H → D, L, P, R or Y: Rifampicin (Rif) resistant. 1 Publication
Mutagenesisi445 – 4451R → L or P: Rifampicin (Rif) resistant. 1 Publication
Mutagenesisi447 – 4471S → L, P or W: Rifampicin (Rif) resistant; RbpA no longer rescues transcription in the presence of Rif, decreased affinity for Rif, no change in affinity for RbpA; tested in the Leu mutation. 2 Publications
Mutagenesisi449 – 4491L → P: Rifampicin (Rif) resistant. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11691169DNA-directed RNA polymerase subunit betaPRO_0000047926Add
BLAST

Interactioni

Subunit structurei

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. Interacts with RbpA, which partially restores Rif-inhibited transcription.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
carDA0R5612EBI-2408357,EBI-2408339

Protein-protein interaction databases

IntActiP60281. 2 interactions.
STRINGi246196.MSMEG_1367.

Structurei

3D structure databases

ProteinModelPortaliP60281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNA polymerase beta chain family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IIJ. Bacteria.
COG0085. LUCA.
HOGENOMiHOG000218611.
KOiK03043.
OMAiYFNPKRY.
OrthoDBiEOG6M9DS6.

Family and domain databases

Gene3Di2.30.150.10. 1 hit.
2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
HAMAPiMF_01321. RNApol_bact_RpoB.
InterProiIPR010243. DNA-dir_RNA_pol_bsu.
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.
IPR014724. RNA_pol_RPB2_OB-fold.
[Graphical view]
PANTHERiPTHR20856. PTHR20856. 3 hits.
PfamiPF04563. 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]
TIGRFAMsiTIGR02013. rpoB. 1 hit.
PROSITEiPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEGCILAVS SQSKSNAITN NSVPGAPNRV SFAKLREPLE VPGLLDVQTD
60 70 80 90 100
SFEWLVGSDR WRQAAIDRGE ENPVGGLEEV LAELSPIEDF SGSMSLSFSD
110 120 130 140 150
PRFDEVKASV DECKDKDMTY AAPLFVTAEF INNNTGEIKS QTVFMGDFPM
160 170 180 190 200
MTEKGTFIIN GTERVVVSQL VRSPGVYFDE TIDKSTEKTL HSVKVIPGRG
210 220 230 240 250
AWLEFDVDKR DTVGVRIDRK RRQPVTVLLK ALGWTNEQIV ERFGFSEIMM
260 270 280 290 300
GTLEKDTTSG TDEALLDIYR KLRPGEPPTK ESAQTLLENL FFKEKRYDLA
310 320 330 340 350
RVGRYKVNKK LGLNAGKPIT SSTLTEEDVV ATIEYLVRLH EGQTSMTVPG
360 370 380 390 400
GVEVPVEVDD IDHFGNRRLR TVGELIQNQI RVGLSRMERV VRERMTTQDV
410 420 430 440 450
EAITPQTLIN IRPVVAAIKE FFGTSQLSQF MDQNNPLSGL THKRRLSALG
460 470 480 490 500
PGGLSRERAG LEVRDVHPSH YGRMCPIETP EGPNIGLIGS LSVYARVNPF
510 520 530 540 550
GFIETPYRKV ENGVVTDQID YLTADEEDRH VVAQANSPTD ENGRFTEDRV
560 570 580 590 600
MVRKKGGEVE FVSADQVDYM DVSPRQMVSV ATAMIPFLEH DDANRALMGA
610 620 630 640 650
NMQRQAVPLV RSEAPLVGTG MELRAAIDAG DVVVADKTGV IEEVSADYIT
660 670 680 690 700
VMADDGTRQS YRLRKFARSN HGTCANQRPI VDAGQRVEAG QVIADGPCTQ
710 720 730 740 750
NGEMALGKNL LVAIMPWEGH NYEDAIILSN RLVEEDVLTS IHIEEHEIDA
760 770 780 790 800
RDTKLGAEEI TRDIPNVSDE VLADLDERGI VRIGAEVRDG DILVGKVTPK
810 820 830 840 850
GETELTPEER LLRAIFGEKA REVRDTSLKV PHGESGKVIG IRVFSREDDD
860 870 880 890 900
ELPAGVNELV RVYVAQKRKI SDGDKLAGRH GNKGVIGKIL PVEDMPFLPD
910 920 930 940 950
GTPVDIILNT HGVPRRMNIG QILETHLGWV AKAGWNIDVA AGVPDWASKL
960 970 980 990 1000
PEELYSAPAD STVATPVFDG AQEGELAGLL GSTLPNRDGE VMVDADGKST
1010 1020 1030 1040 1050
LFDGRSGEPF PYPVTVGYMY ILKLHHLVDD KIHARSTGPY SMITQQPLGG
1060 1070 1080 1090 1100
KAQFGGQRFG EMECWAMQAY GAAYTLQELL TIKSDDTVGR VKVYEAIVKG
1110 1120 1130 1140 1150
ENIPEPGIPE SFKVLLKELQ SLCLNVEVLS SDGAAIEMRD GDDEDLERAA
1160
ANLGINLSRN ESASVEDLA
Length:1,169
Mass (Da):128,531
Last modified:January 16, 2004 - v1
Checksum:iD17F0E28A863FE15
GO

Sequence cautioni

The sequence AFP37801.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ605718 Genomic DNA. Translation: CAE53837.1.
CP000480 Genomic DNA. Translation: ABK70312.1.
CP001663 Genomic DNA. Translation: AFP37801.1. Different initiation.
RefSeqiWP_011727628.1. NZ_CP009494.1.
YP_885753.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK70312; ABK70312; MSMEG_1367.
AFP37801; AFP37801; MSMEI_1328.
GeneIDi4535217.
KEGGimsb:LJ00_06815.
msg:MSMEI_1328.
msm:MSMEG_1367.
PATRICi18075189. VBIMycSme59918_1351.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ605718 Genomic DNA. Translation: CAE53837.1.
CP000480 Genomic DNA. Translation: ABK70312.1.
CP001663 Genomic DNA. Translation: AFP37801.1. Different initiation.
RefSeqiWP_011727628.1. NZ_CP009494.1.
YP_885753.1. NC_008596.1.

3D structure databases

ProteinModelPortaliP60281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP60281. 2 interactions.
STRINGi246196.MSMEG_1367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK70312; ABK70312; MSMEG_1367.
AFP37801; AFP37801; MSMEI_1328.
GeneIDi4535217.
KEGGimsb:LJ00_06815.
msg:MSMEI_1328.
msm:MSMEG_1367.
PATRICi18075189. VBIMycSme59918_1351.

Phylogenomic databases

eggNOGiENOG4108IIJ. Bacteria.
COG0085. LUCA.
HOGENOMiHOG000218611.
KOiK03043.
OMAiYFNPKRY.
OrthoDBiEOG6M9DS6.

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-1367-MONOMER.

Family and domain databases

Gene3Di2.30.150.10. 1 hit.
2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
HAMAPiMF_01321. RNApol_bact_RpoB.
InterProiIPR010243. DNA-dir_RNA_pol_bsu.
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.
IPR014724. RNA_pol_RPB2_OB-fold.
[Graphical view]
PANTHERiPTHR20856. PTHR20856. 3 hits.
PfamiPF04563. 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]
TIGRFAMsiTIGR02013. rpoB. 1 hit.
PROSITEiPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Investigation of drug resistance in Mycobacterium smegmatis using differential gene expression analysis by microarray technology."
    Subramaniyan K., Gopalakrishnakone P.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  4. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  5. "Role of an RNA polymerase interacting protein, MsRbpA, from Mycobacterium smegmatis in phenotypic tolerance to rifampicin."
    Dey A., Verma A.K., Chatterji D.
    Microbiology 156:873-883(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 200-210; 371-381 AND 1149-1159, FUNCTION, INTERACTION WITH RBPA, SUBUNIT, ANTIBIOTIC RESISTANCE, MUTAGENESIS OF ASP-432 AND SER-447.
    Strain: ATCC 700084 / mc(2)155.
  6. "A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria."
    Jain R., Kumar P., Varshney U.
    DNA Repair 6:1774-1785(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANTIBIOTIC RESISTANCE, MUTAGENESIS OF GLN-429; ASP-432; HIS-442; ARG-445; SER-447 AND LEU-449.
    Strain: ATCC 700084 / mc(2)155.

Entry informationi

Entry nameiRPOB_MYCS2
AccessioniPrimary (citable) accession number: P60281
Secondary accession number(s): A0QS65, I7G3Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: November 11, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Mutations in the RRDR sequence (residues 423-449) confer rifampicin (Rif) resistance. Rif blocks transcription inititiation but not elongation.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.