Reviewed, UniProtKB/Swiss-Prot P0A842 (SURE_ECO57)

Names and origin

Protein names

Recommended name:
    Multifunctional protein surE
Including the following 2 domains:
    1- Recommended name:
            5'/3'-nucleotidase
              EC=3.1.3.5
              EC=3.1.3.6
        Alternative name(s):
            Nucleoside monophosphate phosphohydrolase
    2- Recommended name:
            Exopolyphosphatase
              EC=3.6.1.11

Gene names

Name:	surE
Ordered Locus Names:	Z4052, ECs3598

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Sequence similarities	Belongs to the surE nucleotidase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme
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: HAMAP exopolyphosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: HAMAP 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	Multifunctional protein surE HAMAP MF_00060		PRO_0000111810
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)
	P0A842-1 [UniParc]. Last modified June 7, 2005. Version 1. 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]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG57851.1. BA000007 Genomic DNA. Translation: BAB37021.1.
PIR	F91078. G85923.
RefSeq	NP_289293.1. NP_311625.1.
3D structure databases
HSSP	HSSP built from PDB template 1J9L based on UniProtKB P96112.
ModBase	Search...
Genome annotation databases
GeneID	914680. 958038.
GenomeReviews	Gene locus Z4052 in contig AE005174_GR. Gene locus ECs3598 in contig BA000007_GR.
KEGG	ece:Z4052. ecs:ECs3598.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A842.
OMA	P0A842. SINIPIK.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3598-MON.
Family and domain databases
HAMAP	MF_00060. [Tree]
InterPro	IPR002828. SurE-like_Pase/nucleotidase. [Graphical view]
Gene3D	G3DSA:3.40.1210.10. SurE-like_Pase/nucleotidase. 1 hit.
Pfam	PF01975. SurE. 1 hit. [Graphical view]
ProDom	PD005378. SurE. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00087. surE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SURE_ECO57

Accession

Primary (citable) accession number: P0A842
Secondary accession number(s): P36664

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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