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P25814

- RNPA_BACSU

UniProt

P25814 - RNPA_BACSU

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Protein

Ribonuclease P protein component

Gene
rnpA, BSU41050
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  1. tRNA processing Source: UniProtKB-KW
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.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein component (EC:3.1.26.5)
Short name:
RNase P protein
Short name:
RNaseP protein
Alternative name(s):
Protein C5
Gene namesi
Name:rnpA
Ordered Locus Names:BSU41050
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU41050. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 116116Ribonuclease P protein componentUniRule annotationPRO_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.

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 – 53
Helixi10 – 1910
Beta strandi20 – 245
Beta strandi26 – 338
Beta strandi42 – 476
Helixi54 – 7118
Turni72 – 743
Beta strandi79 – 846
Helixi86 – 905
Helixi93 – 10614

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP25814.

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.

Phylogenomic databases

eggNOGiCOG0594.
HOGENOMiHOG000266301.
KOiK03536.
OMAiRKSSLYK.
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

MKKRNRLKKN EDFQKVFKHG TSVANRQFVL YTLDQPENDE LRVGLSVSKK    50
IGNAVMRNRI KRLIRQAFLE EKERLKEKDY IIIARKPASQ LTYEETKKSL 100
QHLFRKSSLY KKSSSK 116
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi I40436. JQ1214.
RefSeqi NP_391985.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A6F X-ray 2.60 A 2-116 [» ]
4JG4 X-ray 2.30 A 2-116 [» ]
DisProti DP00387.
ProteinModelPortali P25814.
SMRi P25814. Positions 1-111.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P25814. 2 interactions.
STRINGi 224308.BSU41050.

Proteomic databases

PaxDbi P25814.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB16142 ; CAB16142 ; BSU41050 .
GeneIDi 937930.
KEGGi bsu:BSU41050.
PATRICi 18980312. VBIBacSub10457_4314.

Organism-specific databases

GenoListi BSU41050. [Micado ]

Phylogenomic databases

eggNOGi COG0594.
HOGENOMi HOG000266301.
KOi K03536.
OMAi RKSSLYK.
OrthoDBi EOG6C01C6.
PhylomeDBi P25814.

Enzyme and pathway databases

BioCyci BSUB:BSU41050-MONOMER.

Miscellaneous databases

EvolutionaryTracei P25814.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
HAMAPi MF_00227. RNase_P.
InterProi IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view ]
Pfami PF00825. Ribonuclease_P. 1 hit.
[Graphical view ]
ProDomi PD003629. Ribonuclease_P. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF54211. SSF54211. 1 hit.
TIGRFAMsi TIGR00188. rnpA. 1 hit.
PROSITEi PS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 113 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

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