UniProtKB - P0A7Z4 (RPOA_ECOLI)
Protein
DNA-directed RNA polymerase subunit alpha
Gene
rpoA
Organism
Escherichia coli (strain K12)
Status
Functioni
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.2 Publications
Part 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 Publication
Catalytic activityi
- EC:2.7.7.6
GO - Molecular functioni
- DNA binding Source: UniProtKB-UniRule
- DNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-UniRule
- protein dimerization activity Source: InterPro
GO - Biological processi
- transcription, DNA-templated Source: UniProtKB-UniRule
Keywordsi
Molecular function | Nucleotidyltransferase, Transferase |
Biological process | Transcription |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10893-MONOMER MetaCyc:EG10893-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: DNA-directed RNA polymerase subunit alpha (EC:2.7.7.6)Short name: RNAP subunit alpha Alternative name(s): RNA polymerase subunit alpha Transcriptase subunit alpha |
Gene namesi | Name:rpoA Synonyms:pez, phs, sez Ordered Locus Names:b3295, JW3257 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
GO - Cellular componenti
Keywords - Cellular componenti
DNA-directed RNA polymerasePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 45 | R → C in rpoA112; temperature-sensitive, blocks RNA polymerase assembly. 1 Publication | 1 | |
Mutagenesisi | 162 – 165 | EEDE → AAAA: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication | 4 | |
Mutagenesisi | 165 | E → K: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication | 1 | |
Mutagenesisi | 191 | R → C in rpoA101; temperature-sensitive. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL2364672 CHEMBL4296169 |
DrugBanki | DB00615, Rifabutin DB11753, Rifamycin |
DrugCentrali | P0A7Z4 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000175304 | 1 – 329 | DNA-directed RNA polymerase subunit alphaAdd BLAST | 329 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 265 | ADP-ribosylarginine1 Publication | 1 | |
Modified residuei | 297 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 298 | N6-acetyllysine; by PatZ1 Publication | 1 |
Post-translational modificationi
Acetylated on Lys-297 and Lys-298 in the presence of glucose. PatZ controls acetylation of Lys-298 but not of Lys-297.1 Publication
(Microbial infection) ADP-ribosylated on both alpha subunits by the phage T4 protein ModA (PubMed:10634320, PubMed:15489438). ADP-ribosylated on only one of the alpha subunits by the phage T4 protein Alt (PubMed:15489438).2 Publications
Keywords - PTMi
Acetylation, ADP-ribosylationProteomic databases
jPOSTi | P0A7Z4 |
PaxDbi | P0A7Z4 |
PRIDEi | P0A7Z4 |
2D gel databases
SWISS-2DPAGEi | P0A7Z4 |
PTM databases
iPTMneti | P0A7Z4 |
Interactioni
Subunit structurei
Homodimer. 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. Both the N- and C-terminus interact with different regions of transcriptional regulator CRP. 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).
6 PublicationsBinary interactionsi
Hide detailsP0A7Z4
With | #Exp. | IntAct |
---|---|---|
coaBC [P0ABQ0] | 2 | EBI-544985,EBI-548929 |
nusA [P0AFF6] | 7 | EBI-544985,EBI-551571 |
rplB [P60422] | 6 | EBI-544985,EBI-543515 |
GO - Molecular functioni
- protein dimerization activity Source: InterPro
Protein-protein interaction databases
BioGRIDi | 4263398, 114 interactors 852106, 1 interactor |
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-35879N |
IntActi | P0A7Z4, 91 interactors |
MINTi | P0A7Z4 |
STRINGi | 511145.b3295 |
Chemistry databases
BindingDBi | P0A7Z4 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A7Z4 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A7Z4 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 235 | Alpha N-terminal domain (alpha-NTD)Add BLAST | 235 | |
Regioni | 162 – 165 | Required for interaction with Crp at class II promoters | 4 | |
Regioni | 249 – 329 | Alpha C-terminal domain (alpha-CTD); not required for RNAP assembly or functionAdd BLAST | 81 |
Domaini
The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators (such as CRP) and with upstream promoter elements.2 Publications
Sequence similaritiesi
Belongs to the RNA polymerase alpha chain family.Curated
Phylogenomic databases
eggNOGi | COG0202, Bacteria |
HOGENOMi | CLU_053084_0_0_6 |
InParanoidi | P0A7Z4 |
PhylomeDBi | P0A7Z4 |
Family and domain databases
Gene3Di | 2.170.120.12, 1 hit 3.30.1360.10, 1 hit |
HAMAPi | MF_00059, RNApol_bact_RpoA, 1 hit |
InterProi | View protein in InterPro IPR011262, DNA-dir_RNA_pol_insert IPR011263, DNA-dir_RNA_pol_RpoA/D/Rpb3 IPR011773, DNA-dir_RpoA IPR036603, RBP11-like IPR011260, RNAP_asu_C IPR036643, RNApol_insert_sf |
Pfami | View protein in Pfam PF01000, RNA_pol_A_bac, 1 hit PF03118, RNA_pol_A_CTD, 1 hit PF01193, RNA_pol_L, 1 hit |
SMARTi | View protein in SMART SM00662, RPOLD, 1 hit |
SUPFAMi | SSF55257, SSF55257, 1 hit SSF56553, SSF56553, 1 hit |
TIGRFAMsi | TIGR02027, rpoA, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A7Z4-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQGSVTEFLK PRLVDIEQVS STHAKVTLEP LERGFGHTLG NALRRILLSS
60 70 80 90 100
MPGCAVTEVE IDGVLHEYST KEGVQEDILE ILLNLKGLAV RVQGKDEVIL
110 120 130 140 150
TLNKSGIGPV TAADITHDGD VEIVKPQHVI CHLTDENASI SMRIKVQRGR
160 170 180 190 200
GYVPASTRIH SEEDERPIGR LLVDACYSPV ERIAYNVEAA RVEQRTDLDK
210 220 230 240 250
LVIEMETNGT IDPEEAIRRA ATILAEQLEA FVDLRDVRQP EVKEEKPEFD
260 270 280 290 300
PILLRPVDDL ELTVRSANCL KAEAIHYIGD LVQRTEVELL KTPNLGKKSL
310 320
TEIKDVLASR GLSLGMRLEN WPPASIADE
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 4 | S → N AA sequence (PubMed:1095419).Curated | 1 | |
Sequence conflicti | 208 | N → T in CAA26395 (PubMed:2989779).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J01685 Genomic DNA Translation: AAA24577.1 X00766 Genomic DNA Translation: CAA25337.1 X02543 Genomic DNA Translation: CAA26395.1 U18997 Genomic DNA Translation: AAA58092.1 X53843 Genomic DNA Translation: CAA37838.1 X53844 Genomic DNA Translation: CAA37839.1 U00096 Genomic DNA Translation: AAC76320.1 AP009048 Genomic DNA Translation: BAE77996.1 V00353 Genomic DNA Translation: CAA23646.1 M29822 Genomic DNA Translation: AAA24590.1 M29823 Genomic DNA Translation: AAA24592.1 M29824 Genomic DNA Translation: AAA24594.1 |
PIRi | A22884, RNECA |
RefSeqi | NP_417754.1, NC_000913.3 WP_001162094.1, NZ_STEB01000038.1 |
Genome annotation databases
EnsemblBacteriai | AAC76320; AAC76320; b3295 BAE77996; BAE77996; BAE77996 |
GeneIDi | 58391067 947794 |
KEGGi | ecj:JW3257 eco:b3295 |
PATRICi | fig|1411691.4.peg.3436 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J01685 Genomic DNA Translation: AAA24577.1 X00766 Genomic DNA Translation: CAA25337.1 X02543 Genomic DNA Translation: CAA26395.1 U18997 Genomic DNA Translation: AAA58092.1 X53843 Genomic DNA Translation: CAA37838.1 X53844 Genomic DNA Translation: CAA37839.1 U00096 Genomic DNA Translation: AAC76320.1 AP009048 Genomic DNA Translation: BAE77996.1 V00353 Genomic DNA Translation: CAA23646.1 M29822 Genomic DNA Translation: AAA24590.1 M29823 Genomic DNA Translation: AAA24592.1 M29824 Genomic DNA Translation: AAA24594.1 |
PIRi | A22884, RNECA |
RefSeqi | NP_417754.1, NC_000913.3 WP_001162094.1, NZ_STEB01000038.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BDF | X-ray | 2.50 | A/B/C/D | 1-235 | [»] | |
1COO | NMR | - | A | 233-329 | [»] | |
1LB2 | X-ray | 3.10 | B/E | 246-329 | [»] | |
1XS9 | NMR | - | D | 249-329 | [»] | |
3IYD | electron microscopy | - | A/B | 1-329 | [»] | |
3K4G | X-ray | 2.05 | A/B/C/D/E/F/G/H | 245-329 | [»] | |
3LU0 | electron microscopy | - | A/B | 1-329 | [»] | |
3N4M | X-ray | 2.99 | B/C | 246-329 | [»] | |
3N97 | X-ray | 3.25 | B/C | 246-329 | [»] | |
4JK1 | X-ray | 3.90 | A/B/F/G | 1-329 | [»] | |
4JK2 | X-ray | 4.20 | A/B/F/G | 1-329 | [»] | |
4KMU | X-ray | 3.85 | A/B/F/G | 1-329 | [»] | |
4KN4 | X-ray | 3.96 | A/B/F/G | 1-329 | [»] | |
4KN7 | X-ray | 3.69 | A/B/F/G | 1-329 | [»] | |
4MEX | X-ray | 3.90 | A/B/G/H | 1-329 | [»] | |
4MEY | X-ray | 3.95 | A/B/G/H | 1-329 | [»] | |
4S20 | X-ray | 4.70 | A/B/F/G | 1-329 | [»] | |
4XSX | X-ray | 3.71 | A/B/G/H | 1-234 | [»] | |
4XSY | X-ray | 4.01 | A/B/G/H | 1-234 | [»] | |
4XSZ | X-ray | 3.68 | A/B/G/H | 1-234 | [»] | |
4YG2 | X-ray | 3.70 | A/B/G/H | 1-329 | [»] | |
4YLN | X-ray | 5.50 | A/B/G/H/M/N | 1-235 | [»] | |
4YLO | X-ray | 6.00 | A/B/G/H/M/N | 1-235 | [»] | |
4YLP | X-ray | 5.50 | A/B/G/H/M/N | 1-235 | [»] | |
4ZH2 | X-ray | 4.20 | A/B/G/H | 2-329 | [»] | |
4ZH3 | X-ray | 4.08 | A/B/G/H | 2-329 | [»] | |
4ZH4 | X-ray | 3.99 | A/B/G/H | 2-329 | [»] | |
5BYH | X-ray | 3.76 | A/B | 1-329 | [»] | |
5CIZ | X-ray | 5.01 | B | 246-329 | [»] | |
5EZK | X-ray | 8.50 | A/B | 1-329 | [»] | |
5IPL | X-ray | 3.60 | A/B | 1-235 | [»] | |
5IPM | X-ray | 4.20 | A/B | 1-235 | [»] | |
5IPN | X-ray | 4.61 | A/B | 1-235 | [»] | |
5MS0 | electron microscopy | 9.80 | A/B | 1-329 | [»] | |
5MY1 | electron microscopy | 7.60 | V/W | 1-329 | [»] | |
5NSR | electron microscopy | 3.80 | A/B | 1-329 | [»] | |
5NSS | electron microscopy | 5.80 | A/B | 1-329 | [»] | |
5NWT | X-ray | 3.76 | A/B | 1-329 | [»] | |
5UAC | X-ray | 3.80 | A/B/G/H | 1-329 | [»] | |
5UAG | X-ray | 3.40 | A/B/G/H | 1-320 | [»] | |
5UAH | X-ray | 4.10 | A/B/G/H | 1-329 | [»] | |
5UAJ | X-ray | 3.92 | A/B/G/H | 1-329 | [»] | |
5UAL | X-ray | 3.89 | A/B/G/H | 1-329 | [»] | |
5UAQ | X-ray | 3.60 | A/B/G/H | 1-329 | [»] | |
5VSW | X-ray | 4.29 | A/B/G/H | 1-329 | [»] | |
5VT0 | electron microscopy | 3.78 | G/H | 1-234 | [»] | |
5W1S | X-ray | 3.81 | A/B/G/H | 1-329 | [»] | |
5W1T | X-ray | 4.50 | A/B/G/H | 1-329 | [»] | |
6ALF | electron microscopy | 4.10 | G/H | 1-234 | [»] | |
6ALG | electron microscopy | 3.70 | G/H | 1-234 | [»] | |
6ALH | electron microscopy | 4.40 | G/H | 1-234 | [»] | |
6ASX | electron microscopy | 3.80 | G/H | 1-234 | [»] | |
6BJS | electron microscopy | 5.50 | G/H | 1-234 | [»] | |
6BYU | X-ray | 3.60 | A/B/G/H | 1-329 | [»] | |
6C6S | electron microscopy | 3.70 | G/H | 1-234 | [»] | |
6C6T | electron microscopy | 3.50 | G/H | 1-234 | [»] | |
6C6U | electron microscopy | 3.70 | G/H | 1-234 | [»] | |
6C9Y | electron microscopy | 4.25 | A/B | 1-329 | [»] | |
6CA0 | electron microscopy | 5.75 | A/B | 1-329 | [»] | |
6CUX | X-ray | 4.10 | A/B/G/H | 1-329 | [»] | |
6FLP | electron microscopy | 4.10 | A/B | 1-329 | [»] | |
6FLQ | electron microscopy | 4.10 | A/B | 1-329 | [»] | |
6GFW | electron microscopy | 3.70 | A/B | 1-329 | [»] | |
6GH5 | electron microscopy | 3.40 | A/B | 1-329 | [»] | |
6GH6 | electron microscopy | 4.10 | A/B | 1-329 | [»] | |
6JBQ | electron microscopy | 4.02 | A/B | 1-329 | [»] | |
6JNX | electron microscopy | 4.08 | A/B | 1-329 | [»] | |
6K4Y | electron microscopy | 3.79 | A/B | 1-329 | [»] | |
6KJ6 | electron microscopy | 3.80 | A/B | 1-329 | [»] | |
6LDI | electron microscopy | 3.69 | A/B | 1-329 | [»] | |
6N4C | electron microscopy | 17.00 | A | 6-321 | [»] | |
B | 6-315 | [»] | ||||
6N57 | electron microscopy | 3.70 | G/H | 1-329 | [»] | |
6N58 | electron microscopy | 3.78 | G/H | 1-329 | [»] | |
6N60 | X-ray | 3.68 | A/B | 1-234 | [»] | |
6N61 | X-ray | 3.25 | A/B | 1-234 | [»] | |
6OMF | electron microscopy | 3.26 | A/B | 1-234 | [»] | |
6OUL | electron microscopy | 3.40 | G/H/R | 1-329 | [»] | |
6P18 | electron microscopy | 3.50 | A/B | 1-329 | [»] | |
6P19 | electron microscopy | 3.80 | A/B | 1-329 | [»] | |
6P1K | electron microscopy | 4.05 | G/H | 1-329 | [»] | |
6PB4 | electron microscopy | 4.35 | A/B | 1-329 | [»] | |
6PB5 | electron microscopy | 4.52 | A/B | 1-329 | [»] | |
6PB6 | electron microscopy | 4.29 | A/B | 1-329 | [»] | |
6PMI | electron microscopy | 3.86 | A/B | 1-329 | [»] | |
6PMJ | electron microscopy | 3.91 | A/B | 1-329 | [»] | |
6PSQ | electron microscopy | 3.40 | G/H/M | 1-329 | [»] | |
6PSR | electron microscopy | 3.40 | G/H/M | 1-329 | [»] | |
6PSS | electron microscopy | 3.50 | G/H/M | 1-329 | [»] | |
6PST | electron microscopy | 3.00 | G/H/M | 1-329 | [»] | |
6PSU | electron microscopy | 3.90 | G/H/M | 1-329 | [»] | |
6PSV | electron microscopy | 3.50 | G/H/M | 1-329 | [»] | |
6PSW | electron microscopy | 3.70 | G/H/M | 1-329 | [»] | |
6R9B | electron microscopy | 3.80 | A/B | 1-329 | [»] | |
6R9G | electron microscopy | 3.70 | A/B | 1-329 | [»] | |
6RH3 | electron microscopy | 3.60 | A/B | 1-329 | [»] | |
6RI7 | electron microscopy | 3.90 | A/B | 1-329 | [»] | |
6RI9 | electron microscopy | 3.70 | A/B | 1-329 | [»] | |
6RIN | electron microscopy | 3.70 | A/B | 1-329 | [»] | |
6RIP | electron microscopy | 3.40 | A/B | 1-329 | [»] | |
6TQN | electron microscopy | 3.80 | U/V | 1-329 | [»] | |
6TQO | electron microscopy | 3.80 | U/V | 1-329 | [»] | |
6UTW | X-ray | 3.85 | AAA/BBB | 1-235 | [»] | |
6UTX | X-ray | 4.05 | AAA/BBB | 1-235 | [»] | |
6UTY | X-ray | 4.15 | AAA/BBB | 1-235 | [»] | |
6UU5 | X-ray | 5.40 | AAA/BBB | 1-235 | [»] | |
6UU6 | X-ray | 4.20 | AAA/BBB | 1-235 | [»] | |
6UU7 | X-ray | 4.40 | AAA/BBB | 1-235 | [»] | |
6UU8 | X-ray | 4.40 | AAA/BBB | 1-235 | [»] | |
6UUB | X-ray | 3.96 | AAA/BBB | 1-235 | [»] | |
6VJS | X-ray | 4.02 | A/B/F/G | 1-329 | [»] | |
6WRG | electron microscopy | 3.58 | A/B | 1-236 | [»] | |
6Z9P | electron microscopy | 3.90 | U/V | 1-329 | [»] | |
6Z9Q | electron microscopy | 5.70 | U/V | 1-329 | [»] | |
6Z9R | electron microscopy | 4.10 | U/V | 1-329 | [»] | |
6Z9S | electron microscopy | 4.40 | U/V | 1-329 | [»] | |
6Z9T | electron microscopy | 4.10 | U/V | 1-329 | [»] | |
6ZTJ | electron microscopy | 3.40 | CA/CB | 1-329 | [»] | |
6ZTL | electron microscopy | 3.50 | CA/CB | 1-329 | [»] | |
6ZTM | electron microscopy | 3.30 | CA/CB | 1-329 | [»] | |
6ZTN | electron microscopy | 3.90 | CA/CB | 1-329 | [»] | |
6ZTO | electron microscopy | 3.00 | CA/CB | 1-329 | [»] | |
6ZTP | electron microscopy | 3.00 | CA/CB | 1-329 | [»] | |
6ZU1 | electron microscopy | 3.00 | CA/CB | 1-329 | [»] | |
7ADB | electron microscopy | 4.40 | U/V | 1-329 | [»] | |
7C17 | electron microscopy | 4.22 | A/B | 1-329 | [»] | |
7KHB | electron microscopy | 3.53 | A/B | 1-329 | [»] | |
7KHC | electron microscopy | 4.14 | A/B | 1-329 | [»] | |
7KHI | electron microscopy | 3.62 | A/B | 1-236 | [»] | |
SMRi | P0A7Z4 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263398, 114 interactors 852106, 1 interactor |
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-35879N |
IntActi | P0A7Z4, 91 interactors |
MINTi | P0A7Z4 |
STRINGi | 511145.b3295 |
Chemistry databases
BindingDBi | P0A7Z4 |
ChEMBLi | CHEMBL2364672 CHEMBL4296169 |
DrugBanki | DB00615, Rifabutin DB11753, Rifamycin |
DrugCentrali | P0A7Z4 |
PTM databases
iPTMneti | P0A7Z4 |
2D gel databases
SWISS-2DPAGEi | P0A7Z4 |
Proteomic databases
jPOSTi | P0A7Z4 |
PaxDbi | P0A7Z4 |
PRIDEi | P0A7Z4 |
Genome annotation databases
EnsemblBacteriai | AAC76320; AAC76320; b3295 BAE77996; BAE77996; BAE77996 |
GeneIDi | 58391067 947794 |
KEGGi | ecj:JW3257 eco:b3295 |
PATRICi | fig|1411691.4.peg.3436 |
Organism-specific databases
EchoBASEi | EB0886 |
Phylogenomic databases
eggNOGi | COG0202, Bacteria |
HOGENOMi | CLU_053084_0_0_6 |
InParanoidi | P0A7Z4 |
PhylomeDBi | P0A7Z4 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10893-MONOMER MetaCyc:EG10893-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0A7Z4 |
PROi | PR:P0A7Z4 |
Family and domain databases
Gene3Di | 2.170.120.12, 1 hit 3.30.1360.10, 1 hit |
HAMAPi | MF_00059, RNApol_bact_RpoA, 1 hit |
InterProi | View protein in InterPro IPR011262, DNA-dir_RNA_pol_insert IPR011263, DNA-dir_RNA_pol_RpoA/D/Rpb3 IPR011773, DNA-dir_RpoA IPR036603, RBP11-like IPR011260, RNAP_asu_C IPR036643, RNApol_insert_sf |
Pfami | View protein in Pfam PF01000, RNA_pol_A_bac, 1 hit PF03118, RNA_pol_A_CTD, 1 hit PF01193, RNA_pol_L, 1 hit |
SMARTi | View protein in SMART SM00662, RPOLD, 1 hit |
SUPFAMi | SSF55257, SSF55257, 1 hit SSF56553, SSF56553, 1 hit |
TIGRFAMsi | TIGR02027, rpoA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RPOA_ECOLI | |
Accessioni | P0A7Z4Primary (citable) accession number: P0A7Z4 Secondary accession number(s): P00574, Q2M6W0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | July 21, 1986 | |
Last modified: | February 10, 2021 | |
This is version 154 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