P0A2X3 (EXOA_STRPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exodeoxyribonuclease
EC=3.1.11.2

Gene names

Name:	exoA
Ordered Locus Names:	SP_1845

Organism

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [Complete proteome] [HAMAP]

Taxonomic identifier

170187 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pneumoniae

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	In addition to 3'- to 5'-exonuclease and 3'-phosphatase activities, ExoA was shown to make single-strand breaks at apurinic sites in DNA By similarity.
Catalytic activity	Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Cofactor	Magnesium. Can also utilize manganese. Probably binds two magnesium or manganese ions per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the DNA repair enzymes AP/ExoA family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Exonuclease Hydrolase Nuclease
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: InterPro nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro endonuclease activity Inferred from electronic annotation. Source: InterPro exodeoxyribonuclease III activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 275	275	Exodeoxyribonuclease		PRO_0000200026
Sites
	Active site	128	1	By similarity
	Active site	167	1	Proton donor/acceptor By similarity
	Metal binding	9	1	Magnesium 1 By similarity
	Metal binding	44	1	Magnesium 1 By similarity
	Metal binding	167	1	Magnesium 2 By similarity
	Metal binding	169	1	Magnesium 2 By similarity
	Metal binding	265	1	Magnesium 1 By similarity
	Site	169	1	Transition state stabilizer By similarity
	Site	240	1	Important for catalytic activity By similarity
	Site	266	1	Interaction with DNA substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A2X3 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 112E5A9FF828A1B9	FASTA	275	31,064
	10 20 30 40 50 60 MKLISWNIDS LNAALTSDSA RAKLSQEVLQ TLVAENADII AIQETKLSAK GPTKKHVEIL 70 80 90 100 110 120 EELFPGYENT WRSSQEPARK GYAGTMFLYK KELTPTISFP EIGAPSTMDL EGRIITLEFD 130 140 150 160 170 180 AFFVTQVYTP NAGDGLKRLE ERQVWDAKYA EYLAELDKEK PVLATGDYNV AHNEIDLANP 190 200 210 220 230 240 ASNRRSPGFT DEERAGFTNL LATGFTDTFR HVHGDVPERY TWWAQRSKTS KINNTGWRID 250 260 270 YWLTSNRIAD KVTKSDMIDS GARQDHTPIV LEIDL

References

[1]

"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae." Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M. Science 293:498-506(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-334 / TIGR4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005672 Genomic DNA. Translation: AAK75918.1.
PIR	E95215.
RefSeq	NP_346278.1. NC_003028.3.
3D structure databases
ProteinModelPortal	P0A2X3.
ModBase	Search...
Protein-protein interaction databases
STRING	170187.SP_1845.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK75918; AAK75918; SP_1845.
GeneID	930987.
KEGG	spn:SP_1845.
PATRIC	19708143. VBIStrPne105772_1914.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0708.
HOGENOM	HOG000034586.
KO	K01142.
OMA	GIRACLK.
ProtClustDB	CLSK2752120.
Family and domain databases
InterPro	IPR020847. AP_endonuclease_F1_BS. IPR020848. AP_endonuclease_F1_CS. IPR005135. Endo/exonuclease/phosphatase. IPR004808. ExoDNase_III. [Graphical view]
PANTHER	PTHR22748. PTHR22748. 1 hit.
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
TIGRFAMs	TIGR00633. xth. 1 hit.
PROSITE	PS00726. AP_NUCLEASE_F1_1. 1 hit. PS00727. AP_NUCLEASE_F1_2. 1 hit. PS00728. AP_NUCLEASE_F1_3. 1 hit. PS51435. AP_NUCLEASE_F1_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EXOA_STRPN

Accession

Primary (citable) accession number: P0A2X3
Secondary accession number(s): P21998

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program