Thermonuclease precursor - Staphylococcus aureus

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P00644 (NUC_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Thermonuclease
Short name=TNase
EC=3.1.31.1

Alternative name(s):
Micrococcal nuclease
Staphylococcal nuclease

Gene names

Name:

nuc

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.
Catalytic activity	Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.
Cofactor	Binds 1 calcium ion per subunit.
Subcellular location	Nuclease A: Secreted. Nuclease B: Membrane.
Sequence similarities	Belongs to the thermonuclease family.
Sequence caution	The sequence AAA26659.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Membrane Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid 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

Signal peptide

1 – 26

Potential

Propeptide

27 – 63

PRO_0000045226

Chain

64 – 231

168

Nuclease B

PRO_0000034389

Propeptide

64 – 82

PRO_0000034390

Chain

83 – 231

149

Nuclease A

PRO_0000034391

Sites

Active site

Active site

Active site

Metal binding

Calcium

Metal binding

122

Calcium

Metal binding

123

Calcium; via carbonyl oxygen

Secondary structure

231

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00644 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: AD5558AA28E855D7
Show »

FASTA

231

25,471

        10         20         30         40         50         60 
MLVMTEYLLS AGICMAIVSI LLIGMAISNV SKGQYAKRFF FFATSCLVLT LVVVSSLSSS 

        70         80         90        100        110        120 
ANASQTDNGV NRSGSEDPTV YSATSTKKLH KEPATLIKAI DGDTVKLMYK GQPMTFRLLL 

       130        140        150        160        170        180 
VDTPETKHPK KGVEKYGPEA SAFTKKMVEN AKKIEVEFDK GQRTDKYGRG LAYIYADGKM 

       190        200        210        220        230 
VNEALVRQGL AKVAYVYKPN NTHEQHLRKS EAQAKKEKLN IWSEDNADSG Q

« Hide

References

[1]	"A genetic system for analysis of staphylococcal nuclease." Shortle D. Gene 22:181-189(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 27735 / Foggie.
[2]	"Secretion of staphylococcal nuclease by Bacillus subtilis." Kovacevic S., Veal L.E., Hsiung H.M., Miller J.R. J. Bacteriol. 162:521-528(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
[3]	"Secretion and processing of staphylococcal nuclease by Bacillus subtilis." Miller J.R., Kovacevic S., Veal L.E. J. Bacteriol. 169:3508-3514(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-63.
[4]	"Nuclease B. A possible precursor of nuclease A, an extracellular nuclease of Staphylococcus aureus." Davis A., Moore I.B., Parker D.S., Taniuchi H. J. Biol. Chem. 252:6544-6553(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 64-82. Strain: ATCC 27735 / Foggie.
[5]	"Staphylococcal nuclease (Foggi strain). II. The amino acid sequence." Cone J.L., Cusumano C.L., Taniuchi H., Anfinsen C.B. J. Biol. Chem. 246:3103-3110(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 83-231. Strain: ATCC 27735 / Foggie.
[6]	"The examination of the presence of amide groups in glutamic acid and aspartic acid residues of staphylococcal nuclease (Foggi strain)." Bohnert J.L., Taniuchi H. J. Biol. Chem. 247:4557-4560(1972) [PubMed] [Europe PMC] [Abstract] Cited for: AMIDE ASSIGNMENTS FOR 83-231. Strain: ATCC 27735 / Foggie.
[7]	"Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3',5'-bisphosphate-calcium ion complex at 1.5-A resolution." Cotton F.A., Hazen E.C. Jr., Legg M.J. Proc. Natl. Acad. Sci. U.S.A. 76:2551-2555(1979) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), PROPOSED CATALYTIC MECHANISM.
[8]	"The crystal structure of staphylococcal nuclease refined at 1.7-A resolution." Hynes T.R., Fox R.O. Proteins 10:92-105(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[9]	"Solution studies of staphylococcal nuclease H124L. 1. Backbone 1H and 15N resonances and secondary structure of the unligated enzyme as identified by three-dimensional NMR spectroscopy." Wang J., Mooberry E.S., Walkenhorst W.F., Markley J.L. Biochemistry 31:911-920(1992) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[10]	"NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease." Shortle D., Abeygunawardana C. Structure 1:121-134(1993) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 83-218.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01281 mRNA. Translation: CAA24594.1.
M17123 Genomic DNA. Translation: AAA26659.1. Different initiation.

PIR

NCSAF. A00790.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A2T	X-ray	1.96	A	83-231	[»]
1A2U	X-ray	2.00	A	83-231	[»]
1A3T	X-ray	2.10	A	83-231	[»]
1A3U	X-ray	2.05	A	83-231	[»]
1A3V	X-ray	2.20	A	83-231	[»]
1AEX	X-ray	2.10	A	83-231	[»]
1ENA	X-ray	2.15	A	89-223	[»]
1ENC	X-ray	1.95	A	83-231	[»]
1EQV	X-ray	1.94	A	88-223	[»]
1EY0	X-ray	1.60	A	83-231	[»]
1EY4	X-ray	1.60	A	83-231	[»]
1EY5	X-ray	1.70	A	83-231	[»]
1EY6	X-ray	1.75	A	83-231	[»]
1EY7	X-ray	1.88	A	83-231	[»]
1EY8	X-ray	1.75	A	83-231	[»]
1EY9	X-ray	1.72	A	83-231	[»]
1EYA	X-ray	2.00	A	83-231	[»]
1EYC	X-ray	1.85	A	83-231	[»]
1EYD	X-ray	1.70	A	83-231	[»]
1EZ6	X-ray	1.90	A	83-231	[»]
1EZ8	X-ray	1.85	A	83-231	[»]
1F2M	X-ray	2.00	A	83-231	[»]
1F2Y	X-ray	2.00	A	83-231	[»]
1F2Z	X-ray	1.80	A	83-231	[»]
1IHZ	X-ray	1.65	A	83-231	[»]
1II3	X-ray	1.72	A	83-231	[»]
1JOK	NMR	-	A	83-231	[»]
1JOO	NMR	-	A	83-231	[»]
1JOQ	NMR	-	A	83-231	[»]
1JOR	NMR	-	A	83-231	[»]
1KAA	X-ray	1.90	A	88-223	[»]
1KAB	X-ray	1.80	A	88-223	[»]
1KDA	X-ray	1.90	A	83-231	[»]
1KDB	X-ray	1.90	A	83-231	[»]
1KDC	X-ray	2.00	A	83-231	[»]
1NSN	X-ray	2.80	S	83-231	[»]
1NUC	X-ray	1.90	A	83-231	[»]
1RKN	NMR	-	A	83-192	[»]
1SNC	X-ray	1.65	A	83-231	[»]
1SND	X-ray	1.84	A/B	83-231	[»]
1SNM	X-ray	1.74	A	83-231	[»]
1SNO	X-ray	1.70	A	83-231	[»]
1SNP	X-ray	1.95	A	83-231	[»]
1SNQ	X-ray	1.70	A	83-231	[»]
1STA	X-ray	1.70	A	83-229	[»]
1STB	X-ray	2.00	A	83-230	[»]
1STG	X-ray	1.70	A	83-231	[»]
1STH	X-ray	1.85	A	83-231	[»]
1STN	X-ray	1.70	A	83-231	[»]
1STY	X-ray	1.67	A	83-230	[»]
1SYB	X-ray	1.80	A	83-231	[»]
1SYC	X-ray	1.80	A	83-231	[»]
1SYD	X-ray	1.70	A	83-231	[»]
1SYE	X-ray	1.80	A	83-231	[»]
1SYF	X-ray	1.80	A	83-231	[»]
1SYG	X-ray	1.90	A	83-231	[»]
1TQO	X-ray	2.00	A	83-226	[»]
1TR5	X-ray	2.10	A	83-226	[»]
1TT2	X-ray	1.85	A	83-226	[»]
1U9R	X-ray	2.10	A	83-231	[»]
2ENB	X-ray	2.05	A	89-223	[»]
2EXZ	X-ray	1.90	A	83-231	[»]
2EY1	X-ray	1.85	A	83-231	[»]
2EY2	X-ray	1.70	A	83-231	[»]
2EY5	X-ray	2.00	A	83-231	[»]
2EY6	X-ray	1.65	A	83-231	[»]
2EYF	X-ray	1.80	A	83-231	[»]
2EYH	X-ray	1.90	A	83-231	[»]
2EYJ	X-ray	1.85	A	83-231	[»]
2EYL	X-ray	1.70	A	83-231	[»]
2EYM	X-ray	1.80	A	83-231	[»]
2EYO	X-ray	1.70	A	83-231	[»]
2EYP	X-ray	1.80	A	83-231	[»]
2F0D	X-ray	2.50	A	83-231	[»]
2F0E	X-ray	1.95	A	83-231	[»]
2F0F	X-ray	2.15	A	83-231	[»]
2F0G	X-ray	1.90	A	83-231	[»]
2F0H	X-ray	2.15	A	83-231	[»]
2F0I	X-ray	1.80	A	83-231	[»]
2F0J	X-ray	1.80	A	83-231	[»]
2F0K	X-ray	1.90	A	83-231	[»]
2F0L	X-ray	1.90	A	83-231	[»]
2F0M	X-ray	2.00	A	83-231	[»]
2F0N	X-ray	1.70	A	83-231	[»]
2F0O	X-ray	1.90	A	83-231	[»]
2F0P	X-ray	2.05	A	83-231	[»]
2F0Q	X-ray	1.95	A	83-231	[»]
2F0S	X-ray	1.75	A	83-231	[»]
2F0T	X-ray	1.70	A	83-231	[»]
2F0U	X-ray	1.83	A	83-231	[»]
2F0V	X-ray	2.00	A	83-231	[»]
2F0W	X-ray	2.10	A	83-231	[»]
2F3V	NMR	-	A	83-192	[»]
2F3W	NMR	-	A	83-192	[»]
2FXY	NMR	-	A	137-154	[»]
2FXZ	NMR	-	A	179-191	[»]
2GSI	X-ray	2.81	W/X/Y/Z	126-136	[»]
2KHS	NMR	-	A	83-203	[»]
2NUC	X-ray	2.00	A	83-231	[»]
2OEO	X-ray	2.00	A	83-226	[»]
2OF1	X-ray	1.92	A	83-226	[»]
2PQE	NMR	-	A	83-231	[»]
2QDB	X-ray	2.20	A	83-231	[»]
2RBM	X-ray	1.90	A	83-231	[»]
2RDF	X-ray	2.01	A	83-231	[»]
2RKS	X-ray	2.01	A	83-231	[»]
2SNM	X-ray	1.97	A	83-231	[»]
2SNS	X-ray	1.50	A	83-231	[»]
2SOB	NMR	-	A	83-185	[»]
3BDC	X-ray	1.80	A	83-231	[»]
3C1E	X-ray	1.90	A	83-231	[»]
3C1F	X-ray	2.00	A	83-231	[»]
3D4D	X-ray	2.10	A/B	83-231	[»]
3D6C	X-ray	2.00	A	83-231	[»]
3DHQ	X-ray	2.15	A	83-231	[»]
3DMU	X-ray	1.80	A	83-231	[»]
3E5S	X-ray	2.00	A/B	83-231	[»]
3EJI	X-ray	1.90	A	83-231	[»]
3ERO	X-ray	1.85	A	83-231	[»]
3ERQ	X-ray	2.10	A	83-231	[»]
3EVQ	X-ray	2.00	A	83-231	[»]
3H6M	X-ray	1.70	A	83-231	[»]
3HEJ	X-ray	1.80	A/B/C/D	83-231	[»]
3HZX	X-ray	2.00	A	83-231	[»]
3ITP	X-ray	1.75	A	83-231	[»]
3LX0	X-ray	1.50	A	83-231	[»]
3MEH	X-ray	1.50	A	83-231	[»]
3MHB	X-ray	1.55	A	83-231	[»]
3MXP	X-ray	1.61	A	83-231	[»]
3MZ5	X-ray	1.58	A	83-231	[»]
3NHH	X-ray	2.00	A	83-231	[»]
3NK9	X-ray	1.65	A	83-231	[»]
3NP8	X-ray	1.70	A	83-231	[»]
3NQT	X-ray	1.90	A	83-231	[»]
3NUC	X-ray	1.90	A	83-231	[»]
3NXW	X-ray	1.65	A	83-231	[»]
3OSO	X-ray	1.60	A	83-231	[»]
3OWF	X-ray	1.85	A	83-231	[»]
3P1H	X-ray	1.79	A	83-231	[»]
3P75	X-ray	1.90	A	89-223	[»]
3PMF	X-ray	1.60	A	83-231	[»]
3QB3	X-ray	1.63	A	83-231	[»]
3RUZ	X-ray	1.58	A	83-231	[»]
3S9W	X-ray	1.90	A	83-231	[»]
3SHL	X-ray	1.48	A	83-231	[»]
3SK4	X-ray	1.85	A	83-231	[»]
3SK5	X-ray	1.70	A	83-231	[»]
3SK6	X-ray	1.80	A	83-231	[»]
3SK8	X-ray	1.90	A	83-231	[»]
3SR1	X-ray	1.45	A	83-231	[»]
3SXH	X-ray	1.40	A	83-231	[»]
3T13	X-ray	1.80	A/B	83-231	[»]
3T16	X-ray	1.80	A	83-231	[»]
3TME	X-ray	1.40	A	83-231	[»]
3TP5	X-ray	1.80	A	83-231	[»]
3TP6	X-ray	1.80	A	83-231	[»]
3TP7	X-ray	1.90	A	83-231	[»]
3TP8	X-ray	1.60	A	83-231	[»]
3U9O	X-ray	1.95	A	83-231	[»]
3V2T	X-ray	1.80	A	83-231	[»]
3VA5	X-ray	1.55	A	83-231	[»]
4DF7	X-ray	1.50	A	83-231	[»]
4DFA	X-ray	1.40	A	83-231	[»]
4DGZ	X-ray	1.47	A	83-231	[»]
4DU9	X-ray	1.63	A	83-231	[»]
4E6I	X-ray	2.00	A/B	83-231	[»]
4EOA	X-ray	1.50	A	83-231	[»]
4EQN	X-ray	1.80	A	83-231	[»]
4EQO	X-ray	1.70	A	83-231	[»]
4EQP	X-ray	1.35	A	83-231	[»]
4EVO	X-ray	1.95	A	83-231	[»]
4F7X	X-ray	1.70	A	83-231	[»]
4F8M	X-ray	1.60	A	83-231	[»]
4G57	X-ray	1.81	A	89-223	[»]
4H7B	X-ray	1.60	A	83-231	[»]
4HMI	X-ray	1.75	A	83-231	[»]
4HMJ	X-ray	1.35	A	83-231	[»]
4HTH	X-ray	1.75	A	83-231	[»]
4IAL	X-ray	1.60	A	83-231	[»]
4ID6	X-ray	1.90	A	83-231	[»]
4IUN	X-ray	1.60	A	83-231	[»]
4IZ8	X-ray	1.70	A	83-231	[»]
4J1M	X-ray	1.65	A	83-231	[»]
4J6H	X-ray	1.60	A	83-231	[»]
5NUC	X-ray	2.10	A	83-231	[»]

DisProt

DP00203.

ProteinModelPortal

P00644.

SMR

P00644. Positions 86-223.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG1525.

Family and domain databases

Gene3D

2.40.50.90. 1 hit.

InterPro

IPR016071. Staphylococal_nuclease_OB-fold.
IPR006021. Staphylococcal_nuclease.
IPR002071. Thermonucl_AS.
[Graphical view]

Pfam

PF00565. SNase. 1 hit.
[Graphical view]

SMART

SM00318. SNc. 1 hit.
[Graphical view]

SUPFAM

SSF50199. Staphylococal_nuclease_OB-fold. 1 hit.

PROSITE

PS01123. TNASE_1. 1 hit.
PS01284. TNASE_2. 1 hit.
PS50830. TNASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01093. Dimethyl sulfoxide.

EvolutionaryTrace

P00644.

Entry information

Entry name

NUC_STAAU

Accession

Primary (citable) accession number: P00644
Secondary accession number(s): P13718, Q53711

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents