Reviewed, UniProtKB/Swiss-Prot P0A0H5 (RNPA_STAAU)

Names and origin

Protein names

Recommended name:
    Ribonuclease P protein component
      Short name=RNaseP protein
      Short name=RNase P protein
    EC=3.1.26.5
Alternative name(s):
    Protein C5

Gene names

Name:

rnpA

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	117 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 MF_00227
Catalytic activity	Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP MF_00227
Subunit structure	Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit. HAMAP MF_00227
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
Gene Ontology (GO)
Biological process	tRNA 5'-leader removal Inferred from electronic annotation. Source: HAMAP
Molecular function	ribonuclease P activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 117

117

Ribonuclease P protein component HAMAP MF_00227

PRO_0000198530

Secondary structure

1

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117

Helix Strand Turn

Details...

Helix

5 – 7

3

Helix

13 – 21

9

Beta strand

27 – 31

5

Beta strand

45 – 48

4

Beta strand

51 – 53

3

Helix

58 – 72

15

Helix

73 – 75

3

Beta strand

82 – 86

5

Helix

89 – 92

4

Helix

97 – 102

6

Helix

105 – 109

5

Beta strand

112 – 114

3

Sequences

	Sequence		Length	Mass (Da)
	P0A0H5-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: AD5172C3654E01F0	FASTA	117	13,652
	10 20 30 40 50 60 MLLEKAYRIK KNADFQRIYK KGHSVANRQF VVYTCNNKEI DHFRLGISVS KKLGNAVLRN 70 80 90 100 110 KIKRAIRENF KVHKSHILAK DIIVIARQPA KDMTTLQIQN SLEHVLKIAK VFNKKIK

References

[1]	"Cloning and characterization of Staphylococcus aureus ribonuclease P." Poppe S.M., Swaney S.M., Choi G.H., Hromockyj A., Shinabarger D.L. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ISP3.
[2]	"The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA." Spitzfaden C., Nicholson N., Jones J.J., Guth S., Lehr R., Prescott C.D., Hegg L.A., Eggleston D.S. J. Mol. Biol. 295:105-115(2000) [PubMed: 10623511] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF135268 Genomic DNA. Translation: AAF61418.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D6T	NMR	-	A	1-117	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.1.26.5. 95.

Family and domain databases

HAMAP

MF_00227.
[Tree]

InterPro

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

Gene3D

G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.

Pfam

PF00825. Ribonuclease_P. 1 hit.
[Graphical view]

ProDom

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

TIGRFAMs

TIGR00188. rnpA. 1 hit.

PROSITE

PS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RNPA_STAAU

Accession

Primary (citable) accession number: P0A0H5
Secondary accession number(s): P58031, Q9LAH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	February 15, 2005
Last modified:	September 22, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)