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P25814

- RNPA_BACSU

UniProt

P25814 - RNPA_BACSU

Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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-EC
    2. tRNA binding Source: InterPro

    GO - Biological processi

    1. tRNA processing Source: UniProtKB-KW

    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 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: 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.1 PublicationUniRule annotation

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25814.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RnpA family.UniRule annotation

    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

    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: October 1, 2014
    This is version 114 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