P25814 (RNPA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	116 AA.
Sequence status	Complete.
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.
Sequence similarities	Belongs to the RnpA family.
Sequence caution	The sequence CAA44400.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	tRNA processing
Ligand	RNA-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ribonuclease P activity Inferred from electronic annotation. Source: EC tRNA binding Inferred from electronic annotation. Source: InterPro
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 [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).
+	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.

PIR

JQ1214. I40436.

RefSeq

NP_391985.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P25814.

SMR

P25814. Positions 1-111.

DisProt

DP00387.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000003043; EBBACP00000003043; EBBACG00000003037.

GeneID

937930.

GenomeReviews

Gene locus BSU41050 in contig AL009126_GR.

KEGG

bsu:BSU41050.

NMPDR

fig|224308.1.peg.4111.

PATRIC

18980312. VBIBacSub10457_4314.

Organism-specific databases

GenoList

BSU41050. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000001736.

HOGENOM

HBG728160.

OMA

KIGNAVM.

PhylomeDB

P25814.

ProtClustDB

PRK00499.

Enzyme and pathway databases

BioCyc

BSUB:BSU41050-MONOMER.

Family and domain databases

HAMAP

MF_00227. RNase_P.
[Tree]

InterPro

IPR020568. Ribosomal_S5_D2-typ_fold.
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.

KO

K03536.

Pfam

PF00825. Ribonuclease_P. 1 hit.
[Graphical view]

ProDom

PD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

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:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program