UniProtKB - P0A8V2 (RPOB_ECOLI)
DNA-directed RNA polymerase subunit beta
rpoB
Functioni
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
2 PublicationsResistance to the antibiotics salinamide A, salinamide B, rifampicin, streptolydigin, CBR703, myxopyronin, and lipiarmycin can result from mutations in this protein.
1 Publication1 PublicationPart of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNAP. It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis.
1 PublicationCatalytic activityi
- EC:2.7.7.6
GO - Molecular functioni
- DNA binding Source: UniProtKB-UniRule
- DNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-UniRule
- ribonucleoside binding Source: InterPro
GO - Biological processi
- regulation of DNA-templated transcription, initiation Source: ComplexPortal
- response to antibiotic Source: UniProtKB-KW
- transcription, DNA-templated Source: UniProtKB-UniRule
- transcription antitermination Source: ComplexPortal
Keywordsi
Molecular function | Nucleotidyltransferase, Transferase |
Biological process | Antibiotic resistance, Transcription |
Enzyme and pathway databases
BioCyci | EcoCyc:RPOB-MONOMER |
BRENDAi | 2.7.7.6, 2026 |
Names & Taxonomyi
Protein namesi | Recommended name: DNA-directed RNA polymerase subunit beta (EC:2.7.7.6)Short name: RNAP subunit beta Alternative name(s): RNA polymerase subunit beta Transcriptase subunit beta |
Gene namesi | Name:rpoB Synonyms:groN, nitB, rif, ron, stl, stv, tabD Ordered Locus Names:b3987, JW3950 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol Source: EcoCyc
- cytosolic DNA-directed RNA polymerase complex Source: ComplexPortal
Other locations
Keywords - Cellular componenti
DNA-directed RNA polymerasePathology & Biotechi
Biotechnological usei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 561 | I → S: Resistant to antibiotics salinamide A and B. 1 Publication | 1 | |
Mutagenesisi | 569 | I → S: Resistant to antibiotics salinamide A and B. 1 Publication | 1 | |
Mutagenesisi | 665 | A → E: Resistant to antibiotics salinamide A and B. 1 Publication | 1 | |
Mutagenesisi | 675 | D → A or G: Resistant to antibiotics salinamide A and B. 1 Publication | 1 | |
Mutagenesisi | 677 | N → H or K: Resistant to antibiotics salinamide A and B. 1 Publication | 1 | |
Mutagenesisi | 680 | L → M: Resistant to antibiotics salinamide A and B. 1 Publication | 1 | |
Mutagenesisi | 813 | E → K: Disrupts the enzyme's active center. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL1852 |
DrugBanki | DB00615, Rifabutin DB04934, Rifalazil DB01045, Rifampicin DB11753, Rifamycin DB01220, Rifaximin |
DrugCentrali | P0A8V2 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000047892 | 1 – 1342 | DNA-directed RNA polymerase subunit betaAdd BLAST | 1342 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1022 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 1200 | N6-acetyllysine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P0A8V2 |
PaxDbi | P0A8V2 |
PRIDEi | P0A8V2 |
2D gel databases
SWISS-2DPAGEi | P0A8V2 |
PTM databases
CarbonylDBi | P0A8V2 |
iPTMneti | P0A8V2 |
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. The rRNA transcription and antitermination complex (rrnTAC) consists of RNAP, NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is more flexible than other subunits (PubMed:32871103).
4 Publications(Microbial infection) Interacts (via flap domain) with Escherichia phage lambda antitermination protein Q; this interaction renders bacterial RNAP resistant to transcription pausing and allows it to read through termination signals.
2 Publications(Microbial infection) Interacts (via flap domain) with the late transcription coactivator of enterobacteria phage T4.
1 PublicationBinary interactionsi
P0A8V2
Protein-protein interaction databases
BioGRIDi | 4263472, 52 interactors 852782, 2 interactors |
ComplexPortali | CPX-4881, DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant CPX-4883, DNA-directed RNA polymerase holoenzyme complex, SigmaS variant CPX-4884, DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant CPX-4885, DNA-directed RNA polymerase holoenzyme complex, SigmaE variant CPX-4886, DNA-directed RNA polymerase holoenzyme complex, SigmaF variant CPX-4887, DNA-directed RNA polymerase holoenzyme complex, SigmaH variant CPX-4888, DNA-directed RNA polymerase holoenzyme complex, Sigma fecI variant CPX-5674, Transcription elongation complex CPX-5780, lambdaN-dependent processive transcription antitermination complex |
DIPi | DIP-35777N |
IntActi | P0A8V2, 103 interactors |
STRINGi | 511145.b3987 |
Chemistry databases
BindingDBi | P0A8V2 |
Structurei
Secondary structure
3D structure databases
SMRi | P0A8V2 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A8V2 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0085, Bacteria |
HOGENOMi | CLU_000524_4_3_6 |
InParanoidi | P0A8V2 |
PhylomeDBi | P0A8V2 |
Family and domain databases
CDDi | cd00653, RNA_pol_B_RPB2, 1 hit |
Gene3Di | 2.30.150.10, 1 hit 2.40.270.10, 1 hit 2.40.50.150, 1 hit 3.90.1110.10, 1 hit |
HAMAPi | MF_01321, RNApol_bact_RpoB, 1 hit |
InterProi | View protein in InterPro IPR042107, DNA-dir_RNA_pol_bsu_ext_1_sf IPR019462, DNA-dir_RNA_pol_bsu_external_1 IPR015712, DNA-dir_RNA_pol_su2 IPR007120, DNA-dir_RNAP_su2_dom IPR037033, DNA-dir_RNAP_su2_hyb_sf IPR010243, RNA_pol_bsu_bac IPR007121, RNA_pol_bsu_CS IPR007644, RNA_pol_bsu_protrusion IPR007642, RNA_pol_Rpb2_2 IPR037034, RNA_pol_Rpb2_2_sf IPR007645, RNA_pol_Rpb2_3 IPR007641, RNA_pol_Rpb2_7 IPR014724, RNA_pol_RPB2_OB-fold |
PANTHERi | PTHR20856, PTHR20856, 1 hit |
Pfami | View protein in Pfam PF04563, RNA_pol_Rpb2_1, 1 hit PF04561, RNA_pol_Rpb2_2, 2 hits 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 |
TIGRFAMsi | TIGR02013, rpoB, 1 hit |
PROSITEi | View protein in PROSITE PS01166, RNA_POL_BETA, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MVYSYTEKKR IRKDFGKRPQ VLDVPYLLSI QLDSFQKFIE QDPEGQYGLE
60 70 80 90 100
AAFRSVFPIQ SYSGNSELQY VSYRLGEPVF DVQECQIRGV TYSAPLRVKL
110 120 130 140 150
RLVIYEREAP EGTVKDIKEQ EVYMGEIPLM TDNGTFVING TERVIVSQLH
160 170 180 190 200
RSPGVFFDSD KGKTHSSGKV LYNARIIPYR GSWLDFEFDP KDNLFVRIDR
210 220 230 240 250
RRKLPATIIL RALNYTTEQI LDLFFEKVIF EIRDNKLQME LVPERLRGET
260 270 280 290 300
ASFDIEANGK VYVEKGRRIT ARHIRQLEKD DVKLIEVPVE YIAGKVVAKD
310 320 330 340 350
YIDESTGELI CAANMELSLD LLAKLSQSGH KRIETLFTND LDHGPYISET
360 370 380 390 400
LRVDPTNDRL SALVEIYRMM RPGEPPTREA AESLFENLFF SEDRYDLSAV
410 420 430 440 450
GRMKFNRSLL REEIEGSGIL SKDDIIDVMK KLIDIRNGKG EVDDIDHLGN
460 470 480 490 500
RRIRSVGEMA ENQFRVGLVR VERAVKERLS LGDLDTLMPQ DMINAKPISA
510 520 530 540 550
AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR ERAGFEVRDV
560 570 580 590 600
HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRKVTDGVVT
610 620 630 640 650
DEIHYLSAIE EGNYVIAQAN SNLDEEGHFV EDLVTCRSKG ESSLFSRDQV
660 670 680 690 700
DYMDVSTQQV VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV
710 720 730 740 750
GTGMERAVAV DSGVTAVAKR GGVVQYVDAS RIVIKVNEDE MYPGEAGIDI
760 770 780 790 800
YNLTKYTRSN QNTCINQMPC VSLGEPVERG DVLADGPSTD LGELALGQNM
810 820 830 840 850
RVAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELACVS RDTKLGPEEI
860 870 880 890 900
TADIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK
910 920 930 940 950
LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQVFTRDGVE KDKRALEIEE
960 970 980 990 1000
MQLKQAKKDL SEELQILEAG LFSRIRAVLV AGGVEAEKLD KLPRDRWLEL
1010 1020 1030 1040 1050
GLTDEEKQNQ LEQLAEQYDE LKHEFEKKLE AKRRKITQGD DLAPGVLKIV
1060 1070 1080 1090 1100
KVYLAVKRRI QPGDKMAGRH GNKGVISKIN PIEDMPYDEN GTPVDIVLNP
1110 1120 1130 1140 1150
LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQQQEVAK LREFIQRAYD
1160 1170 1180 1190 1200
LGADVRQKVD LSTFSDEEVM RLAENLRKGM PIATPVFDGA KEAEIKELLK
1210 1220 1230 1240 1250
LGDLPTSGQI RLYDGRTGEQ FERPVTVGYM YMLKLNHLVD DKMHARSTGS
1260 1270 1280 1290 1300
YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG
1310 1320 1330 1340
RTKMYKNIVD GNHQMEPGMP ESFNVLLKEI RSLGINIELE DE
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 4 | S → R AA sequence (PubMed:1095419).Curated | 1 | |
Sequence conflicti | 106 – 107 | ER → G in CAA23629 (PubMed:7011900).Curated | 2 | |
Sequence conflicti | 384 – 391 | LFENLFFS → CSRTCSSPT in CAA23629 (PubMed:7011900).Curated | 8 | |
Sequence conflicti | 516 | D → V in CAA23625 (PubMed:6266829).Curated | 1 | |
Sequence conflicti | 516 | D → V in CAA23627 (PubMed:6266829).Curated | 1 | |
Sequence conflicti | 516 | D → V in AAA24585 (Ref. 11) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V00339 Genomic DNA Translation: CAA23625.1 V00340 Genomic DNA Translation: CAA23627.1 U76222 Genomic DNA Translation: AAB18647.1 U00006 Genomic DNA Translation: AAC43085.1 U00096 Genomic DNA Translation: AAC76961.1 AP009048 Genomic DNA Translation: BAE77333.1 V00341 Genomic DNA Translation: CAA23629.1 M38292 Genomic DNA Translation: AAA24579.1 M38293 Genomic DNA Translation: AAA24581.1 M38287 Genomic DNA Translation: AAA24585.1 M38304 Genomic DNA Translation: AAA24580.1 U77436 Genomic DNA Translation: AAD09605.1 M38303 Genomic DNA Translation: AAA24583.1 |
PIRi | F65205, RNECB |
RefSeqi | NP_418414.1, NC_000913.3 WP_000263098.1, NZ_STEB01000045.1 |
Genome annotation databases
EnsemblBacteriai | AAC76961; AAC76961; b3987 BAE77333; BAE77333; BAE77333 |
GeneIDi | 67415312 948488 |
KEGGi | ecj:JW3950 eco:b3987 |
PATRICi | fig|1411691.4.peg.2725 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V00339 Genomic DNA Translation: CAA23625.1 V00340 Genomic DNA Translation: CAA23627.1 U76222 Genomic DNA Translation: AAB18647.1 U00006 Genomic DNA Translation: AAC43085.1 U00096 Genomic DNA Translation: AAC76961.1 AP009048 Genomic DNA Translation: BAE77333.1 V00341 Genomic DNA Translation: CAA23629.1 M38292 Genomic DNA Translation: AAA24579.1 M38293 Genomic DNA Translation: AAA24581.1 M38287 Genomic DNA Translation: AAA24585.1 M38304 Genomic DNA Translation: AAA24580.1 U77436 Genomic DNA Translation: AAD09605.1 M38303 Genomic DNA Translation: AAA24583.1 |
PIRi | F65205, RNECB |
RefSeqi | NP_418414.1, NC_000913.3 WP_000263098.1, NZ_STEB01000045.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3IYD | electron microscopy | - | C | 1-1342 | [»] | |
3LTI | X-ray | 1.60 | A | 152-443 | [»] | |
3LU0 | electron microscopy | - | C | 1-1342 | [»] | |
3T72 | X-ray | 4.33 | o/q | 896-910 | [»] | |
3TBI | X-ray | 3.00 | B | 831-1057 | [»] | |
4JK1 | X-ray | 3.90 | C/H | 1-1342 | [»] | |
4JK2 | X-ray | 4.20 | C/H | 1-1342 | [»] | |
4KMU | X-ray | 3.85 | C/H | 1-1342 | [»] | |
4KN4 | X-ray | 3.96 | C/H | 1-1342 | [»] | |
4KN7 | X-ray | 3.69 | C/H | 1-1342 | [»] | |
4MEX | X-ray | 3.90 | C/I | 1-1342 | [»] | |
4MEY | X-ray | 3.95 | C/I | 1-1342 | [»] | |
4S20 | X-ray | 4.70 | C/H | 1-1342 | [»] | |
4XSX | X-ray | 3.71 | C/I | 1-1342 | [»] | |
4XSY | X-ray | 4.01 | C/I | 1-1342 | [»] | |
4XSZ | X-ray | 3.68 | C/I | 1-1342 | [»] | |
4YG2 | X-ray | 3.70 | C/I | 1-1342 | [»] | |
4YLN | X-ray | 5.50 | C/I/O | 1-1342 | [»] | |
4YLO | X-ray | 6.00 | C/I/O | 1-1342 | [»] | |
4YLP | X-ray | 5.50 | C/I/O | 1-1342 | [»] | |
4ZH2 | X-ray | 4.20 | C/I | 1-1342 | [»] | |
4ZH3 | X-ray | 4.08 | C/I | 1-1342 | [»] | |
4ZH4 | X-ray | 3.99 | C/I | 1-1342 | [»] | |
5BYH | X-ray | 3.76 | C | 1-1342 | [»] | |
5EZK | X-ray | 8.50 | C | 1-1342 | [»] | |
5IPL | X-ray | 3.60 | C | 1-1342 | [»] | |
5IPM | X-ray | 4.20 | C | 1-1342 | [»] | |
5IPN | X-ray | 4.61 | C | 1-1342 | [»] | |
5MS0 | electron microscopy | 9.80 | C | 1-1342 | [»] | |
5MY1 | electron microscopy | 7.60 | X | 1-1342 | [»] | |
5NSR | electron microscopy | 3.80 | C | 1-1342 | [»] | |
5NSS | electron microscopy | 5.80 | C | 1-1342 | [»] | |
5NWT | X-ray | 3.76 | C | 1-1342 | [»] | |
5UAC | X-ray | 3.80 | C/I | 1-1342 | [»] | |
5UAG | X-ray | 3.40 | C/I | 1-1342 | [»] | |
5UAH | X-ray | 4.10 | C/I | 1-1342 | [»] | |
5UAJ | X-ray | 3.92 | C/I | 1-1342 | [»] | |
5UAL | X-ray | 3.89 | C/I | 1-1342 | [»] | |
5UAQ | X-ray | 3.60 | C/I | 1-1342 | [»] | |
5VSW | X-ray | 4.29 | C/I | 1-1342 | [»] | |
5VT0 | electron microscopy | 3.78 | I | 1-1342 | [»] | |
5W1S | X-ray | 3.81 | C/I | 1-1342 | [»] | |
5W1T | X-ray | 4.50 | C/I | 1-1342 | [»] | |
6ALF | electron microscopy | 4.10 | I | 1-1342 | [»] | |
6ALG | electron microscopy | 3.70 | I | 1-1342 | [»] | |
6ALH | electron microscopy | 4.40 | I | 1-1342 | [»] | |
6ASX | electron microscopy | 3.80 | I | 1-1342 | [»] | |
6BJS | electron microscopy | 5.50 | I | 1-1342 | [»] | |
6BYU | X-ray | 3.60 | C/I | 1-1342 | [»] | |
6C6S | electron microscopy | 3.70 | I | 1-1342 | [»] | |
6C6T | electron microscopy | 3.50 | I | 1-1342 | [»] | |
6C6U | electron microscopy | 3.70 | I | 1-1342 | [»] | |
6C9Y | electron microscopy | 4.25 | C | 1-1342 | [»] | |
6CA0 | electron microscopy | 5.75 | C | 1-1342 | [»] | |
6CUX | X-ray | 4.10 | C/I | 1-1342 | [»] | |
6FLP | electron microscopy | 4.10 | C | 1-1342 | [»] | |
6FLQ | electron microscopy | 4.10 | C | 1-1342 | [»] | |
6GFW | electron microscopy | 3.70 | C | 1-1342 | [»] | |
6GH5 | electron microscopy | 3.40 | C | 1-1342 | [»] | |
6GH6 | electron microscopy | 4.10 | C | 1-1342 | [»] | |
6JBQ | electron microscopy | 4.02 | C | 1-1342 | [»] | |
6JNX | electron microscopy | 4.08 | C | 1-1342 | [»] | |
6K4Y | electron microscopy | 3.79 | C | 1-1342 | [»] | |
6KJ6 | electron microscopy | 3.80 | C | 1-1342 | [»] | |
6LDI | electron microscopy | 3.69 | C | 1-1342 | [»] | |
6N4C | electron microscopy | 17.00 | C | 2-1342 | [»] | |
6N57 | electron microscopy | 3.70 | I | 1-1342 | [»] | |
6N58 | electron microscopy | 3.78 | I | 1-1342 | [»] | |
6N60 | X-ray | 3.68 | C | 1-1342 | [»] | |
6N61 | X-ray | 3.25 | C | 1-1342 | [»] | |
6OMF | electron microscopy | 3.26 | C | 1-1342 | [»] | |
6OUL | electron microscopy | 3.40 | I | 1-1342 | [»] | |
6P18 | electron microscopy | 3.50 | C | 1-1342 | [»] | |
6P19 | electron microscopy | 3.80 | C | 1-1342 | [»] | |
6P1K | electron microscopy | 4.05 | I | 1-1342 | [»] | |
6PSQ | electron microscopy | 3.40 | I | 1-1342 | [»] | |
6PSR | electron microscopy | 3.40 | I | 1-1342 | [»] | |
6PSS | electron microscopy | 3.50 | I | 1-1342 | [»] | |
6PST | electron microscopy | 3.00 | I | 1-1342 | [»] | |
6PSU | electron microscopy | 3.90 | I | 1-1342 | [»] | |
6PSV | electron microscopy | 3.50 | I | 1-1342 | [»] | |
6PSW | electron microscopy | 3.70 | I | 1-1342 | [»] | |
6R9B | electron microscopy | 3.80 | C | 1-1342 | [»] | |
6R9G | electron microscopy | 3.70 | C | 1-1342 | [»] | |
6RH3 | electron microscopy | 3.60 | C | 1-1342 | [»] | |
6RI7 | electron microscopy | 3.90 | C | 1-1342 | [»] | |
6RI9 | electron microscopy | 3.70 | C | 1-1342 | [»] | |
6RIN | electron microscopy | 3.70 | C | 1-1342 | [»] | |
6RIP | electron microscopy | 3.40 | C | 1-1342 | [»] | |
6TQN | electron microscopy | 3.80 | X | 1-1342 | [»] | |
6TQO | electron microscopy | 4.00 | X | 1-1342 | [»] | |
6UTV | X-ray | 3.45 | CCC | 1-1342 | [»] | |
6VJS | X-ray | 4.02 | C/H | 1-1342 | [»] | |
6WMU | electron microscopy | 3.18 | C | 1-1342 | [»] | |
6X26 | electron microscopy | 4.10 | I | 1-1342 | [»] | |
6X2F | electron microscopy | 4.00 | I | 1-1342 | [»] | |
6X2N | electron microscopy | 3.90 | I | 1-1342 | [»] | |
6X43 | electron microscopy | 3.60 | I | 1-1342 | [»] | |
6X4W | electron microscopy | 3.80 | I | 1-1342 | [»] | |
6X4Y | electron microscopy | 3.60 | I | 1-1342 | [»] | |
6X50 | electron microscopy | 3.30 | I | 1-1342 | [»] | |
6XAS | electron microscopy | 3.80 | I | 1-1342 | [»] | |
6XAV | electron microscopy | 7.70 | I | 1-1342 | [»] | |
6XH7 | electron microscopy | 3.90 | C | 1-1342 | [»] | |
6XH8 | electron microscopy | 4.10 | C | 1-1342 | [»] | |
6XL5 | electron microscopy | 2.50 | C | 1-1342 | [»] | |
6XL9 | electron microscopy | 2.50 | C | 1-1342 | [»] | |
6XLJ | electron microscopy | 2.70 | C | 1-1342 | [»] | |
6XLL | electron microscopy | 2.70 | C | 1-1342 | [»] | |
6XLM | electron microscopy | 3.20 | C | 1-1342 | [»] | |
6XLN | electron microscopy | 2.80 | C | 1-1342 | [»] | |
6Z9P | electron microscopy | 3.90 | X | 1-1342 | [»] | |
6Z9Q | electron microscopy | 5.70 | X | 1-1342 | [»] | |
6Z9R | electron microscopy | 4.10 | X | 1-1342 | [»] | |
6Z9S | electron microscopy | 4.40 | X | 1-1342 | [»] | |
6Z9T | electron microscopy | 4.10 | X | 1-1342 | [»] | |
6ZTL | electron microscopy | 3.50 | CC | 1-1342 | [»] | |
7ADB | electron microscopy | 4.40 | X | 1-1342 | [»] | |
7ADC | electron microscopy | 4.00 | X | 1-1342 | [»] | |
7ADD | electron microscopy | 4.30 | X | 1-1342 | [»] | |
7ADE | electron microscopy | 4.20 | X | 1-1342 | [»] | |
7C17 | electron microscopy | 4.22 | C | 1-1342 | [»] | |
7C97 | electron microscopy | 3.68 | C | 1-1342 | [»] | |
7CHW | electron microscopy | 3.58 | C | 1-1342 | [»] | |
7KHB | electron microscopy | 3.53 | C | 1-1342 | [»] | |
7KHC | electron microscopy | 4.14 | C | 1-1342 | [»] | |
7KHE | electron microscopy | 3.58 | C | 1-1342 | [»] | |
7KHI | electron microscopy | 3.62 | C | 1-1342 | [»] | |
7MKN | electron microscopy | 3.30 | C | 3-1342 | [»] | |
7MKO | electron microscopy | 3.15 | C | 3-1342 | [»] | |
7MKQ | electron microscopy | 4.80 | C | 3-1342 | [»] | |
SMRi | P0A8V2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263472, 52 interactors 852782, 2 interactors |
ComplexPortali | CPX-4881, DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant CPX-4883, DNA-directed RNA polymerase holoenzyme complex, SigmaS variant CPX-4884, DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant CPX-4885, DNA-directed RNA polymerase holoenzyme complex, SigmaE variant CPX-4886, DNA-directed RNA polymerase holoenzyme complex, SigmaF variant CPX-4887, DNA-directed RNA polymerase holoenzyme complex, SigmaH variant CPX-4888, DNA-directed RNA polymerase holoenzyme complex, Sigma fecI variant CPX-5674, Transcription elongation complex CPX-5780, lambdaN-dependent processive transcription antitermination complex |
DIPi | DIP-35777N |
IntActi | P0A8V2, 103 interactors |
STRINGi | 511145.b3987 |
Chemistry databases
BindingDBi | P0A8V2 |
ChEMBLi | CHEMBL1852 |
DrugBanki | DB00615, Rifabutin DB04934, Rifalazil DB01045, Rifampicin DB11753, Rifamycin DB01220, Rifaximin |
DrugCentrali | P0A8V2 |
PTM databases
CarbonylDBi | P0A8V2 |
iPTMneti | P0A8V2 |
2D gel databases
SWISS-2DPAGEi | P0A8V2 |
Proteomic databases
jPOSTi | P0A8V2 |
PaxDbi | P0A8V2 |
PRIDEi | P0A8V2 |
Genome annotation databases
EnsemblBacteriai | AAC76961; AAC76961; b3987 BAE77333; BAE77333; BAE77333 |
GeneIDi | 67415312 948488 |
KEGGi | ecj:JW3950 eco:b3987 |
PATRICi | fig|1411691.4.peg.2725 |
Organism-specific databases
EchoBASEi | EB0887 |
Phylogenomic databases
eggNOGi | COG0085, Bacteria |
HOGENOMi | CLU_000524_4_3_6 |
InParanoidi | P0A8V2 |
PhylomeDBi | P0A8V2 |
Enzyme and pathway databases
BioCyci | EcoCyc:RPOB-MONOMER |
BRENDAi | 2.7.7.6, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0A8V2 |
PROi | PR:P0A8V2 |
Family and domain databases
CDDi | cd00653, RNA_pol_B_RPB2, 1 hit |
Gene3Di | 2.30.150.10, 1 hit 2.40.270.10, 1 hit 2.40.50.150, 1 hit 3.90.1110.10, 1 hit |
HAMAPi | MF_01321, RNApol_bact_RpoB, 1 hit |
InterProi | View protein in InterPro IPR042107, DNA-dir_RNA_pol_bsu_ext_1_sf IPR019462, DNA-dir_RNA_pol_bsu_external_1 IPR015712, DNA-dir_RNA_pol_su2 IPR007120, DNA-dir_RNAP_su2_dom IPR037033, DNA-dir_RNAP_su2_hyb_sf IPR010243, RNA_pol_bsu_bac IPR007121, RNA_pol_bsu_CS IPR007644, RNA_pol_bsu_protrusion IPR007642, RNA_pol_Rpb2_2 IPR037034, RNA_pol_Rpb2_2_sf IPR007645, RNA_pol_Rpb2_3 IPR007641, RNA_pol_Rpb2_7 IPR014724, RNA_pol_RPB2_OB-fold |
PANTHERi | PTHR20856, PTHR20856, 1 hit |
Pfami | View protein in Pfam PF04563, RNA_pol_Rpb2_1, 1 hit PF04561, RNA_pol_Rpb2_2, 2 hits 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 |
TIGRFAMsi | TIGR02013, rpoB, 1 hit |
PROSITEi | View protein in PROSITE PS01166, RNA_POL_BETA, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RPOB_ECOLI | |
Accessioni | P0A8V2Primary (citable) accession number: P0A8V2 Secondary accession number(s): P00575 Q2M8S3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | June 7, 2005 | |
Last modified: | February 23, 2022 | |
This is version 159 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families