B8YB65 · RPO13_SACSH

Function

function

DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (Probable). A molten-globule protein, it binds dsDNA in the RNAP, in vitro binds dsDNA but not ssDNA (Probable) (PubMed:22848102).
Its position in RNAP implies it functions in both transcription initiation and elongation (Probable)

Catalytic activity

Features

Showing features for binding site.

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TypeIDPosition(s)Description
Binding site32DNA (UniProtKB | ChEBI); template DNA

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentDNA-directed RNA polymerase complex
Molecular FunctionDNA binding
Molecular Functionnucleotidyltransferase activity
Molecular FunctionRNA polymerase binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA-directed RNA polymerase subunit Rpo13
  • EC number

Gene names

    • Name
      rpo13
    • ORF names
      J5U23_03039

Organism names

Accessions

  • Primary accession
    B8YB65
  • Secondary accessions
    • A0A8F5GUL2

Proteomes

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis1-33Decreased stability, still binds DNA.
Mutagenesis81-104Protein is stable, no longer binds DNA.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004537881-104DNA-directed RNA polymerase subunit Rpo13

Interaction

Subunit

Part of the 13-subunit RNA polymerase complex. Rpo1N and Rpo5 form a cleft which docks Rpo13 (PubMed:19419240, PubMed:21265742, PubMed:22848102).
Forms predominantly dimers in solution, although monomers and trimers can also be seen (PubMed:21265742, PubMed:22848102).
Found associated with RNAP but also as a homodimer pool in the cytoplasm in vivo (PubMed:22848102).

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region1-34Disordered
Compositional bias11-28Acidic residues
Region76-104Disordered
Region81-104Required to bind DNA
Compositional bias83-97Basic residues

Domain

Forms a helix-turn-helix motif with helix 1 (residues 38-56) nearly parallel to helix 2 (residues 61-82); helix 1 contacts both Rpo5 and Rpo1N. The C-terminal region (residues 81-104) is required for DNA-binding.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    104
  • Mass (Da)
    12,148
  • Last updated
    2009-03-03 v1
  • MD5 Checksum
    691466EED6990FEA51C61EF1D30D59EC
MVSGMSTEEEKEGTNDEEVSEEREVEETSEEEFPKLSIQDIELLMKNTEIWDNLLNGKISVDEAKRLFEDNYKDYEKRDSRRKAKKAASKKVKKTKKKEKSVEG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias11-28Acidic residues
Compositional bias83-97Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FJ515677
EMBL· GenBank· DDBJ
ACL36500.1
EMBL· GenBank· DDBJ
Genomic DNA
CP077717
EMBL· GenBank· DDBJ
QXJ30148.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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