Q1R7U7 (SURE_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5'/3'-nucleotidase SurE
EC=3.1.3.5
EC=3.1.3.6

Alternative name(s):
Exopolyphosphatase
EC=3.6.1.11
Nucleoside monophosphate phosphohydrolase

Gene names

Name:	surE
Ordered Locus Names:	UTI89_C3115

Organism

Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

364106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs By similarity. HAMAP MF_00060
Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP MF_00060 A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP MF_00060 (Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate. HAMAP MF_00060
Cofactor	Binds 1 divalent metal cation per subunit By similarity.
Subcellular location	Cytoplasm Potential HAMAP MF_00060.
Sequence similarities	Belongs to the surE nucleotidase family.
Sequence caution	The sequence ABE08567.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3'-nucleotidase activity Inferred from electronic annotation. Source: EC 5'-nucleotidase activity Inferred from electronic annotation. Source: EC exopolyphosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide 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 – 253	253	5'/3'-nucleotidase SurE HAMAP MF_00060		PRO_0000335260
Sites
	Metal binding	8	1	Divalent metal cation By similarity
	Metal binding	9	1	Divalent metal cation By similarity
	Metal binding	39	1	Divalent metal cation By similarity
	Metal binding	92	1	Divalent metal cation By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1R7U7 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: 33A7CD0AEE13C3DB	FASTA	253	26,900
	10 20 30 40 50 60 MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD 70 80 90 100 110 120 IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA 130 140 150 160 170 180 LAVSLDGHKH YDTAAAVTCS ILRALCKEPL RTGRILNINV PDLPLDQIKG IRVTRCGTRH 190 200 210 220 230 240 PADQVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV 250 SDWLNSVGVG TQW

References

[1]

"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UTI89 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000243 Genomic DNA. Translation: ABE08567.1. Different initiation.
RefSeq	YP_542098.1. NC_007946.1.
3D structure databases
ProteinModelPortal	Q1R7U7.
SMR	Q1R7U7. Positions 1-253.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1R7U7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000067592; EBESCP00000065070; EBESCG00000066639.
GeneID	3994212.
GenomeReviews	Gene locus UTI89_C3115 in contig CP000243_GR.
KEGG	eci:UTI89_C3115.
PATRIC	18455750. VBIEscCol42261_3097.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0496.
GeneTree	EBGT00050000011302.
HOGENOM	HBG600532.
OMA	KHTASAG.
ProtClustDB	PRK00346.
Enzyme and pathway databases
BioCyc	ECOL364106:UTI89_C3115-MONOMER.
Family and domain databases
HAMAP	MF_00060. SurE. [Tree]
InterPro	IPR002828. SurE-like_Pase/nucleotidase. [Graphical view]
Gene3D	G3DSA:3.40.1210.10. SurE-like_Pase/nucleotidase. 1 hit.
KO	K03787.
Pfam	PF01975. SurE. 1 hit. [Graphical view]
SUPFAM	SSF64167. SurE-like_Pase/nucleotidase. 1 hit.
TIGRFAMs	TIGR00087. SurE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SURE_ECOUT

Accession

Primary (citable) accession number: Q1R7U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	January 25, 2012
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program