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P25814 (RNPA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:BSU41050
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length116 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence caution

The sequence CAA44400.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processtRNA processing
   LigandRNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 116116Ribonuclease P protein component HAMAP-Rule MF_00227
PRO_0000198424

Secondary structure

................... 116
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25814 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: E15CA6B7851716BE

FASTA11613,800
        10         20         30         40         50         60 
MKKRNRLKKN EDFQKVFKHG TSVANRQFVL YTLDQPENDE LRVGLSVSKK IGNAVMRNRI 

        70         80         90        100        110 
KRLIRQAFLE EKERLKEKDY IIIARKPASQ LTYEETKKSL QHLFRKSSLY KKSSSK 

« Hide

References

« Hide 'large scale' references
[1]"Genes and their organization in the replication origin region of the bacterial chromosome."
Ogasawara N., Yoshikawa H.
Mol. Microbiol. 6:629-634(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / CRK2000.
[2]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Structure and function of the spoIIIJ gene of Bacillus subtilis: a vegetatively expressed gene that is essential for sigma G activity at an intermediate stage of sporulation."
Errington J., Appleby L., Daniel R.A., Goodfellow H., Partridge S.R., Yudkin M.D.
J. Gen. Microbiol. 138:2609-2618(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-116.
Strain: 168.
[5]"Expression, purification and characterization of the recombinant ribonuclease P protein component from Bacillus subtilis."
Niranjanakumari S., Kurz J.C., Fierke C.A.
Nucleic Acids Res. 26:3090-3096(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Ribonuclease P protein structure: evolutionary origins in the translational apparatus."
Stams T., Niranjanakumari S., Fierke C.A., Christianson D.W.
Science 280:752-755(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62539 Genomic DNA. Translation: CAA44400.1. Different initiation.
D26185 Genomic DNA. Translation: BAA05235.1.
AL009126 Genomic DNA. Translation: CAB16142.1.
Z14225 Genomic DNA. Translation: CAA78594.1.
PIRJQ1214. I40436.
RefSeqNP_391985.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6FX-ray2.60A2-116[»]
4JG4X-ray2.30A2-116[»]
DisProtDP00387.
ProteinModelPortalP25814.
SMRP25814. Positions 1-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP25814. 2 interactions.
STRING224308.BSU41050.

Proteomic databases

PaxDbP25814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB16142; CAB16142; BSU41050.
GeneID937930.
KEGGbsu:BSU41050.
PATRIC18980312. VBIBacSub10457_4314.

Organism-specific databases

GenoListBSU41050. [Micado]

Phylogenomic databases

eggNOGCOG0594.
HOGENOMHOG000266301.
KOK03536.
OMARKSSLYK.
OrthoDBEOG6C01C6.
PhylomeDBP25814.

Enzyme and pathway databases

BioCycBSUB:BSU41050-MONOMER.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
HAMAPMF_00227. RNase_P.
InterProIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view]
PfamPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
ProDomPD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR00188. rnpA. 1 hit.
PROSITEPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25814.

Entry information

Entry nameRNPA_BACSU
AccessionPrimary (citable) accession number: P25814
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList