Descriptions

The DNA-dependent RNA polymerase (RNAP) is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living organisms. In bacteria, RNAP is responsible for the synthesis of all RNAs in the cell (messenger RNA, ribosomal RNA, transfer RNA, and so on). The bacterial RNAP exists in two forms: core and holoenzyme. The core enzyme has a relative molecular mass of about 400,000, and consists of five subunits: α-dimer (α2), β, β' and ω. They are evolutionarily conserved in sequence, structure and function from bacteria to humans. The binding of initiation factor σ to a RNAP core enzyme results in the formation of a holoenzyme, the active form of RNAP essential for transcription initiation. The atomic model of the σ70 subunit lacks the disordered N-terminal domain (σ1-73), which includes the conserved σ region 1.1. This is a self-inhibitory domain, which is known to mask the DNA-binding regions of σ before it binds the core.

Autoinhibitory domains (AIDs)

Target domain

187-256 (Sigma-70 factor domain-2); 357-409 (Sigma-70 factor domain-4)

Relief mechanism

Partner binding

Assay

Mutagenesis experiment, Deletion assay, Structural analysis

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

3 structures for Q72L95

Entry ID Method Resolution Chain Position Source
1IW7 X-ray 260 A F/P 1-423 PDB
1SMY X-ray 270 A F/P 1-423 PDB
AF-Q72L95-F1 Predicted AlphaFoldDB

No variants for Q72L95

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q72L95

No associated diseases with Q72L95

10 regional properties for Q72L95

Type Name Position InterPro Accession
domain RNA polymerase sigma-70 211 - 224 IPR000943-1
domain RNA polymerase sigma-70 235 - 243 IPR000943-2
domain RNA polymerase sigma-70 361 - 373 IPR000943-3
domain RNA polymerase sigma-70 382 - 408 IPR000943-4
domain RNA polymerase sigma-70 region 3 266 - 344 IPR007624
domain RNA polymerase sigma-70 region 2 187 - 256 IPR007627
domain RNA polymerase sigma-70 region 4 357 - 409 IPR007630
domain RNA polymerase sigma-70 region 1.2 79 - 112 IPR009042
domain RNA polymerase sigma factor RpoD, C-terminal 183 - 422 IPR012760
domain RNA polymerase sigma-70 like domain 183 - 409 IPR014284

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family PTHR30603 RNA POLYMERASE SIGMA FACTOR RPO
PANTHER Subfamily PTHR30603:SF47 RNA POLYMERASE SIGMA FACTOR SIGF, CHLOROPLASTIC
PANTHER Protein Class helix-turn-helix transcription factor
Sigma factor
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
sigma factor activity Sigma factors act as the promoter specificity subunit of eubacterial and plant plastid multisubunit RNA polymerases, whose core subunit composition is often described as alpha(2)-beta-beta-prime. Although sigma does not bind DNA on its own, when combined with the core to form the holoenzyme, the sigma factor binds specifically to promoter elements. The sigma subunit is released once elongation begins.

1 GO annotations of biological process

Name Definition
DNA-templated transcription, initiation The initial step of transcription, consisting of the assembly of the RNA polymerase preinitiation complex (PIC) at a gene promoter, as well as the formation of the first few bonds of the RNA transcript. Transcription initiation includes abortive initiation events, which occur when the first few nucleotides are repeatedly synthesized and then released, and ends when promoter clearance takes place.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKKSKRKNAQ AQEAQETEVL VQEEAEELPE FPEGEPDPDL EDPDLALEDD LLDLPEEGEG
70 80 90 100 110 120
LDLEEEEEDL PIPKISTSDP VRQYLHEIGQ VPLLTLEEEV ELARKVEEGM EAIKKLSEIT
130 140 150 160 170 180
GLDPDLIREV VRAKILGSAR VRHIPGLKET LDPKTVEEID QKLKSLPKEH KRYLHIAREG
190 200 210 220 230 240
EAARQHLIEA NLRLVVSIAK KYTGRGLSFL DLIQEGNQGL IRAVEKFEYK RRFKFSTYAT
250 260 270 280 290 300
WWIRQAINRA IADQARTIRI PVHMVETINK LSRTARQLQQ ELGREPTYEE IAEAMGPGWD
310 320 330 340 350 360
AKRVEETLKI AQEPVSLETP IGDEKDSFYG DFIPDEHLPS PVDAATQSLL SEELEKALSK
370 380 390 400 410 420
LSEREAMVLK LRKGLIDGRE HTLEEVGAFF GVTRERIRQI ENKALRKLKY HESRTRKLRD
FLD