P0A840 (SURE_ECOLI) 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
Stationary-phase survival protein SurE

Gene names

Name:	surE
Synonyms:	ygbC
Ordered Locus Names:	b2744, JW2714

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Also plays a significant physiological role in stress-response and is required for the survival of E.coli in stationary growth phase. Ref.5
Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP-Rule MF_00060 A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP-Rule MF_00060 (Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate. HAMAP-Rule MF_00060
Cofactor	Binds 1 divalent metal cation per subunit. Highest nucleotidase activity with Mn2+, followed by Co2+, Ni2+ and Mg2+. Highest exopolyphosphatase activity with Mg2+, followed by Co2+ and Zn2+. Ref.5
Enzyme regulation	Inhibited by various ribo- or deoxyribonucleoside 5'-triphosphates but is insensitive to nucleoside diphosphates. HAMAP-Rule MF_00060
Subunit structure	Monomer and homooligomer in solution. The oligomeric complex consists of at least four subunits. Ref.5
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00060.
Sequence similarities	Belongs to the SurE nucleotidase family.
Caution	Was originally annotated as an acid phosphatase (EC 3.1.3.2).
Biophysicochemical properties	Kinetic parameters: KM=0.32 mM for 5'-AMP Ref.5 KM=0.26 mM for 5'-GMP KM=0.28 mM for 5'-dGMP KM=0.10 mM for 3'-AMP KM=0.37 mM for 3'-CMP KM=2.49 mM for pNPP KM=0.02 mM for polyphosphate Vmax=10.0 µmol/min/mg enzyme with 5'-AMP as substrate Vmax=22.4 µmol/min/mg enzyme with 5'-GMP as substrate Vmax=16.4 µmol/min/mg enzyme with 5'-dGMP as substrate Vmax=20.1 µmol/min/mg enzyme with 3'-AMP as substrate Vmax=12.1 µmol/min/mg enzyme with 3'-CMP as substrate Vmax=7.24 µmol/min/mg enzyme with pNPP as substrate Vmax=0.10 µmol/min/mg enzyme with polyphosphate as substrate pH dependence: Optimum pH is 7.0-7.2 for nucleotidase activity.
Sequence caution	The sequence AAA69254.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cobalt Magnesium Manganese Metal-binding Nickel Nucleotide-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Inferred from mutant phenotype PubMed 9785447. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3'-nucleotidase activity Inferred from direct assay Ref.5. Source: EcoCyc 5'-nucleotidase activity Inferred from direct assay Ref.5. Source: EcoCyc exopolyphosphatase activity Inferred from direct assay Ref.5. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
betA	P17444	1	EBI-1126761,EBI-1115667

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 253	253	5'/3'-nucleotidase SurE HAMAP-Rule MF_00060		PRO_0000111809
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)
	P0A840 [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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome." Li C., Ichikawa J.K., Ravetto J.J., Kuo H.-C., Fu J.C., Clarke S. J. Bacteriol. 176:6015-6022(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MP180.
[2]	Ichikawa J.K. Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG." Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F. J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CHARACTERIZATION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L07942 Genomic DNA. Translation: AAA79839.1. U29579 Genomic DNA. Translation: AAA69254.1. Different initiation. U00096 Genomic DNA. Translation: AAC75786.1. AP009048 Genomic DNA. Translation: BAE76821.1.
PIR	I69732.
RefSeq	NP_417224.1. NC_000913.2. YP_490953.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0A840.
SMR	P0A840. Positions 1-253.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47982N.
IntAct	P0A840. 3 interactions.
STRING	511145.b2744.
Proteomic databases
PaxDb	P0A840.
PRIDE	P0A840.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75786; AAC75786; b2744. BAE76821; BAE76821; BAE76821.
GeneID	12933283. 947211.
KEGG	ecj:Y75_p2682. eco:b2744.
PATRIC	32120894. VBIEscCol129921_2839.
Organism-specific databases
EchoBASE	EB1764.
EcoGene	EG11817. surE.
Phylogenomic databases
eggNOG	COG0496.
HOGENOM	HOG000122500.
KO	K03787.
OMA	IASEVWI.
ProtClustDB	PRK00346.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11817-MONOMER. ECOL316407:JW2714-MONOMER. MetaCyc:EG11817-MONOMER.
BRENDA	3.1.3.5. 2026.
SABIO-RK	P0A840.
Gene expression databases
Genevestigator	P0A840.
Family and domain databases
Gene3D	3.40.1210.10. 1 hit.
HAMAP	MF_00060. SurE.
InterPro	IPR002828. SurE-like_Pase/nucleotidase. [Graphical view]
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_ECOLI

Accession

Primary (citable) accession number: P0A840
Secondary accession number(s): P36664, Q2MA85

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program