Ribonuclease P protein component - Escherichia coli (strain K12)

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P0A7Y8 (RNPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribonuclease P protein component
Short name=RNase P protein
Short name=RNaseP protein
EC=3.1.26.5

Alternative name(s):
Protein C5

Gene names

Name:	rnpA
Ordered Locus Names:	b3704, JW3681

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	119 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. HAMAP-Rule MF_00227
Catalytic activity	Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00227
Subunit structure	Consists of a catalytic RNA component (M1 or RnpB) and a protein subunit.
Sequence similarities	Belongs to the RnpA family.

Ontologies

Keywords
Biological process	tRNA processing
Ligand	RNA-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA 5'-leader removal Inferred from direct assay PubMed 167017. Source: EcoliWiki
Molecular_function	ribonuclease P activity Inferred from direct assay PubMed 7509797. Source: EcoCyc tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 119

119

Ribonuclease P protein component HAMAP-Rule MF_00227

PRO_0000198458

Secondary structure

119

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7Y8 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 449D9EDACA1C6240
Show »

FASTA

119

13,789

        10         20         30         40         50         60 
MVKLAFPREL RLLTPSQFTF VFQQPQRAGT PQITILGRLN SLGHPRIGLT VAKKNVRRAH 

        70         80         90        100        110 
ERNRIKRLTR ESFRLRQHEL PAMDFVVVAK KGVADLDNRA LSEALEKLWR RHCRLARGS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Physical mapping and nucleotide sequence of the rnpA gene that encodes the protein component of ribonuclease P in Escherichia coli." Hansen F.G., Hansen E.B., Atlung T. Gene 38:85-93(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R. Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The nucleotide sequence of the dnaA gene promoter and of the adjacent rpmH gene, coding for the ribosomal protein L34, of Escherichia coli." Hansen F.G., Hansen E.B., Atlung T. EMBO J. 1:1043-1048(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M11056 Genomic DNA. Translation: AAA24567.1.
X01861 Genomic DNA. Translation: CAA25983.1.
L10328 Genomic DNA. Translation: AAA62055.1.
U00096 Genomic DNA. Translation: AAC76727.1.
AP009048 Genomic DNA. Translation: BAE77590.1.

PIR

NRECP. A00794.

RefSeq

NP_418159.1. NC_000913.2.
YP_491731.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LJP	NMR	-	A	1-119	[»]

ProteinModelPortal

P0A7Y8.

SMR

P0A7Y8. Positions 1-119.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36039N.

IntAct

P0A7Y8. 54 interactions.

MINT

MINT-1218365.

STRING

511145.b3704.

Proteomic databases

PaxDb

P0A7Y8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76727; AAC76727; b3704.
BAE77590; BAE77590; BAE77590.

GeneID

12932772.
948215.

KEGG

ecj:Y75_p3469.
eco:b3704.

PATRIC

32122905. VBIEscCol129921_3828.

Organism-specific databases

EchoBASE

EB0855.

EcoGene

EG10862. rnpA.

Phylogenomic databases

eggNOG

COG0594.

HOGENOM

HOG000266301.

K03536.

OMA

HFKAVFD.

ProtClustDB

PRK01732.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10862-MONOMER.
ECOL316407:JW3681-MONOMER.
MetaCyc:EG10862-MONOMER.

Gene expression databases

Genevestigator

P0A7Y8.

Family and domain databases

Gene3D

3.30.230.10. 1 hit.

HAMAP

MF_00227. RNase_P.

InterPro

IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view]

Pfam

PF00825. Ribonuclease_P. 1 hit.
[Graphical view]

ProDom

PD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

TIGRFAMs

TIGR00188. rnpA. 1 hit.

PROSITE

PS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2043.

Entry information

Entry name

RNPA_ECOLI

Accession

Primary (citable) accession number: P0A7Y8
Secondary accession number(s): P06277, Q2M816

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 29, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents