Reviewed, UniProtKB/Swiss-Prot P25814 (RNPA_BACSU)

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
Ordered Locus Names:	BSU41050

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	116 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 Complete proteome
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 – 116

116

Ribonuclease P protein component HAMAP MF_00227

PRO_0000198424

Secondary structure

1

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116

Helix Strand Turn

Details...

Helix

3 – 5

3

Helix

10 – 19

10

Beta strand

20 – 24

5

Beta strand

26 – 32

7

Beta strand

42 – 47

6

Helix

54 – 71

18

Turn

72 – 74

3

Beta strand

77 – 84

8

Helix

86 – 88

3

Helix

93 – 106

14

Sequences

	Sequence		Length	Mass (Da)
	P25814-1 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: E15CA6B7851716BE	FASTA	116	13,800
	10 20 30 40 50 60 MKKRNRLKKN EDFQKVFKHG TSVANRQFVL YTLDQPENDE LRVGLSVSKK IGNAVMRNRI 70 80 90 100 110 KRLIRQAFLE EKERLKEKDY IIIARKPASQ LTYEETKKSL QHLFRKSSLY KKSSSK

References

	« Hide 'large scale' referencesShow '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: 1552862] [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: 7584024] [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: 9384377] [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: 1487728] [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: 9628904] [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: 9563955] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

JQ1214. I40436.

RefSeq

NP_391985.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A6F	X-ray	2.60	A	2-116	[»]

DisProt

DP00387.

ModBase

Search...

Genome annotation databases

GeneID

937930.

GenomeReviews

Gene locus BSU41050 in contig AL009126_GR.

KEGG

bsu:BSU41050.

NMPDR

fig|224308.1.peg.4111.

Organism-specific databases

SubtiList

BG10063. rnpA. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P25814.

OMA

KRRIRQS.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU4102-MON.

BRENDA

3.1.26.5. 150.

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_BACSU

Accession

Primary (citable) accession number: P25814

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	October 1, 1994
Last modified:	November 3, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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