Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.UniRule annotation

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-HAMAP
  2. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. tRNA 5'-leader removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU41050-MONOMER.
BRENDAi3.1.26.5. 658.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein componentUniRule annotation (EC:3.1.26.5UniRule annotation)
Short name:
RNase P proteinUniRule annotation
Short name:
RNaseP proteinUniRule annotation
Alternative name(s):
Protein C5UniRule annotation
Gene namesi
Name:rnpAUniRule annotation
Ordered Locus Names:BSU41050
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU41050. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 116116Ribonuclease P protein componentPRO_0000198424Add
BLAST

Proteomic databases

PaxDbiP25814.

Interactioni

Subunit structurei

Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit. Might be a component of the prossible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno, and possibly also rnpA. Interacts with RNA helicase CshA.UniRule annotation1 Publication

Protein-protein interaction databases

IntActiP25814. 2 interactions.
STRINGi224308.BSU41050.

Structurei

Secondary structure

1
116
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi10 – 1910Combined sources
Beta strandi20 – 245Combined sources
Beta strandi26 – 338Combined sources
Beta strandi42 – 476Combined sources
Helixi54 – 7118Combined sources
Turni72 – 743Combined sources
Beta strandi79 – 846Combined sources
Helixi86 – 905Combined sources
Helixi93 – 10614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6FX-ray2.60A2-116[»]
4JG4X-ray2.30A2-116[»]
DisProtiDP00387.
ProteinModelPortaliP25814.
SMRiP25814. Positions 1-111.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25814.

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0594.
HOGENOMiHOG000266301.
InParanoidiP25814.
KOiK03536.
OMAiRWVREAW.
OrthoDBiEOG6C01C6.
PhylomeDBiP25814.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00227. RNase_P.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view]
PfamiPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
ProDomiPD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR00188. rnpA. 1 hit.
PROSITEiPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25814-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRNRLKKN EDFQKVFKHG TSVANRQFVL YTLDQPENDE LRVGLSVSKK
60 70 80 90 100
IGNAVMRNRI KRLIRQAFLE EKERLKEKDY IIIARKPASQ LTYEETKKSL
110
QHLFRKSSLY KKSSSK
Length:116
Mass (Da):13,800
Last modified:October 1, 1994 - v2
Checksum:iE15CA6B7851716BE
GO

Sequence cautioni

The sequence CAA44400.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI40436. JQ1214.
RefSeqiNP_391985.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB16142; CAB16142; BSU41050.
GeneIDi937930.
KEGGibsu:BSU41050.
PATRICi18980312. VBIBacSub10457_4314.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI40436. JQ1214.
RefSeqiNP_391985.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6FX-ray2.60A2-116[»]
4JG4X-ray2.30A2-116[»]
DisProtiDP00387.
ProteinModelPortaliP25814.
SMRiP25814. Positions 1-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP25814. 2 interactions.
STRINGi224308.BSU41050.

Proteomic databases

PaxDbiP25814.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB16142; CAB16142; BSU41050.
GeneIDi937930.
KEGGibsu:BSU41050.
PATRICi18980312. VBIBacSub10457_4314.

Organism-specific databases

GenoListiBSU41050. [Micado]

Phylogenomic databases

eggNOGiCOG0594.
HOGENOMiHOG000266301.
InParanoidiP25814.
KOiK03536.
OMAiRWVREAW.
OrthoDBiEOG6C01C6.
PhylomeDBiP25814.

Enzyme and pathway databases

BioCyciBSUB:BSU41050-MONOMER.
BRENDAi3.1.26.5. 658.

Miscellaneous databases

EvolutionaryTraceiP25814.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00227. RNase_P.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view]
PfamiPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
ProDomiPD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR00188. rnpA. 1 hit.
PROSITEiPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "Characterization of components of the Staphylococcus aureus mRNA degradosome holoenzyme-like complex."
    Roux C.M., DeMuth J.P., Dunman P.M.
    J. Bacteriol. 193:5520-5526(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSHA, SUBUNIT.
  7. "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).

Entry informationi

Entry nameiRNPA_BACSU
AccessioniPrimary (citable) accession number: P25814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 1, 1994
Last modified: April 1, 2015
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.