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Protein

DNA-directed RNA polymerase subunit alpha

Gene

rpoA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processTranscription

Enzyme and pathway databases

BioCyciEcoCyc: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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10893 rpoA

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB

Keywords - Cellular componenti

DNA-directed RNA polymerase

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45R → C in rpoA112; temperature-sensitive, blocks RNA polymerase assembly. 1 Publication1
Mutagenesisi162 – 165EEDE → AAAA: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication4
Mutagenesisi165E → K: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication1
Mutagenesisi191R → C in rpoA101; temperature-sensitive. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2364672
DrugBankiDB00615 Rifabutin

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001753041 – 329DNA-directed RNA polymerase subunit alphaAdd BLAST329

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei297N6-acetyllysine1 Publication1
Modified residuei298N6-acetyllysine; by Pka1 Publication1

Post-translational modificationi

Acetylated on Lys-297 and Lys-298 in the presence of glucose. Pka controls acetylation of Lys-298 but not of Lys-297.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A7Z4
PaxDbiP0A7Z4
PRIDEiP0A7Z4

2D gel databases

SWISS-2DPAGEiP0A7Z4

PTM databases

iPTMnetiP0A7Z4

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.4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4263398, 114 interactors
852106, 1 interactor
DIPiDIP-35879N
IntActiP0A7Z4, 91 interactors
MINTiP0A7Z4
STRINGi316385.ECDH10B_3470

Chemistry databases

BindingDBiP0A7Z4

Structurei

Secondary structure

1329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 32Combined sources20
Helixi35 – 47Combined sources13
Beta strandi54 – 61Combined sources8
Beta strandi74 – 76Combined sources3
Helixi78 – 86Combined sources9
Beta strandi96 – 111Combined sources16
Helixi112 – 114Combined sources3
Beta strandi122 – 124Combined sources3
Beta strandi129 – 133Combined sources5
Beta strandi139 – 148Combined sources10
Beta strandi151 – 153Combined sources3
Helixi155 – 157Combined sources3
Beta strandi170 – 172Combined sources3
Beta strandi179 – 186Combined sources8
Beta strandi196 – 207Combined sources12
Beta strandi209 – 211Combined sources3
Helixi213 – 227Combined sources15
Helixi228 – 231Combined sources4
Helixi251 – 254Combined sources4
Helixi257 – 260Combined sources4
Helixi264 – 270Combined sources7
Turni271 – 274Combined sources4
Helixi278 – 283Combined sources6
Helixi286 – 290Combined sources5
Beta strandi292 – 294Combined sources3
Helixi297 – 299Combined sources3
Helixi300 – 303Combined sources4
Helixi308 – 310Combined sources3
Beta strandi318 – 322Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BDFX-ray2.50A/B/C/D1-235[»]
1COONMR-A233-329[»]
1LB2X-ray3.10B/E246-329[»]
1XS9NMR-D249-329[»]
3IYDelectron microscopy-A/B1-329[»]
3K4GX-ray2.05A/B/C/D/E/F/G/H245-329[»]
3LU0electron microscopy-A/B1-329[»]
3N4MX-ray2.99B/C246-329[»]
3N97X-ray3.25B/C246-329[»]
4JK1X-ray3.90A/B/F/G1-329[»]
4JK2X-ray4.20A/B/F/G1-329[»]
4KMUX-ray3.85A/B/F/G1-329[»]
4KN4X-ray3.96A/B/F/G1-329[»]
4KN7X-ray3.69A/B/F/G1-329[»]
4MEXX-ray3.90A/B/G/H1-329[»]
4MEYX-ray3.95A/B/G/H1-329[»]
4S20X-ray4.70A/B/F/G1-329[»]
4XSXX-ray3.71A/B/G/H1-234[»]
4XSYX-ray4.01A/B/G/H1-234[»]
4XSZX-ray3.68A/B/G/H1-234[»]
4YG2X-ray3.70A/B/G/H1-329[»]
4YLNX-ray5.50A/B/G/H/M/N1-235[»]
4YLOX-ray6.00A/B/G/H/M/N1-235[»]
4YLPX-ray5.50A/B/G/H/M/N1-235[»]
4ZH2X-ray4.20A/B/G/H2-329[»]
4ZH3X-ray4.08A/B/G/H2-329[»]
4ZH4X-ray3.99A/B/G/H2-329[»]
5BYHX-ray3.76A/B1-329[»]
5CIZX-ray5.01B246-329[»]
5EZKX-ray8.50A/B1-329[»]
5IPLX-ray3.60A/B1-235[»]
5IPMX-ray4.20A/B1-235[»]
5IPNX-ray4.61A/B1-235[»]
5MS0electron microscopy9.80A/B1-329[»]
5MY1electron microscopy7.60V/W1-329[»]
5NSRelectron microscopy3.80A/B1-329[»]
5NSSelectron microscopy5.80A/B1-329[»]
5NWTX-ray3.76A/B1-329[»]
5UACX-ray3.80A/B/G/H1-329[»]
5UAGX-ray3.40A/B/G/H1-320[»]
5UAHX-ray4.10A/B/G/H1-329[»]
5UAJX-ray3.92A/B/G/H1-329[»]
5UALX-ray3.89A/B/G/H1-329[»]
5UAQX-ray3.60A/B/G/H1-329[»]
5VSWX-ray4.29A/B/G/H1-329[»]
5VT0electron microscopy3.78G/H1-234[»]
5W1SX-ray3.81A/B/G/H1-329[»]
5W1TX-ray4.50A/B/G/H1-329[»]
6ALFelectron microscopy4.10G/H1-234[»]
6ALGelectron microscopy3.70G/H1-234[»]
6ALHelectron microscopy4.40G/H1-234[»]
6ASXelectron microscopy3.80G/H1-234[»]
6BJSelectron microscopy5.50G/H1-234[»]
6BYUX-ray3.60A/B/G/H1-329[»]
6C9Yelectron microscopy4.25A/B1-329[»]
6CA0electron microscopy5.75A/B1-329[»]
6FLPelectron microscopy4.10A/B1-329[»]
6FLQelectron microscopy4.10A/B1-329[»]
ProteinModelPortaliP0A7Z4
SMRiP0A7Z4
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7Z4

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 235Alpha N-terminal domain (alpha-NTD)Add BLAST235
Regioni162 – 165Required for interaction with Crp at class II promoters4
Regioni249 – 329Alpha C-terminal domain (alpha-CTD); not required for RNAP assembly or functionAdd BLAST81

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

eggNOGiCOG0202 LUCA
HOGENOMiHOG000218481
InParanoidiP0A7Z4
KOiK03040
OMAiLMKFRNF
PhylomeDBiP0A7Z4

Family and domain databases

Gene3Di2.170.120.12, 1 hit
3.30.1360.10, 2 hits
HAMAPiMF_00059 RNApol_bact_RpoA, 1 hit
InterProiView 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
PANTHERiPTHR32108 PTHR32108, 1 hit
PfamiView protein in Pfam
PF01000 RNA_pol_A_bac, 1 hit
PF03118 RNA_pol_A_CTD, 1 hit
PF01193 RNA_pol_L, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001179 RNAP_asu_C, 1 hit
SMARTiView protein in SMART
SM00662 RPOLD, 1 hit
SUPFAMiSSF55257 SSF55257, 2 hits
SSF56553 SSF56553, 1 hit
TIGRFAMsiTIGR02027 rpoA, 1 hit

Sequencei

Sequence statusi: Complete.

P0A7Z4-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:329
Mass (Da):36,512
Last modified:July 21, 1986 - v1
Checksum:i12A14B75A3CAEA19
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4S → N AA sequence (PubMed:1095419).Curated1
Sequence conflicti208N → T in CAA26395 (PubMed:2989779).Curated1

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
PIRiA22884 RNECA
RefSeqiNP_417754.1, NC_000913.3
WP_001162094.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76320; AAC76320; b3295
BAE77996; BAE77996; BAE77996
GeneIDi947794
KEGGiecj:JW3257
eco:b3295
PATRICifig|1411691.4.peg.3436

Similar proteinsi

Entry informationi

Entry nameiRPOA_ECOLI
AccessioniPrimary (citable) accession number: P0A7Z4
Secondary accession number(s): P00574, Q2M6W0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 23, 2018
This is version 132 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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