Multifunctional protein surE - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A840 (SURE_ECOLI)

Last modified June 16, 2009. Version 34. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Multifunctional protein surE
Alternative name(s):
    Stationary-phase survival 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
Synonyms:	ygbC
Ordered Locus Names:	b2744, JW2714

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 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. 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 MF_00060
Subunit structure	Monomer and homooligomer in solution. The oligomeric complex consists of at least four subunits. Ref.5
Subcellular location	Cytoplasm Potential.
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: K_M=0.32 mM for 5'-AMP HAMAP MF_00060 K_M=0.26 mM for 5'-GMP K_M=0.28 mM for 5'-dGMP K_M=0.10 mM for 3'-AMP K_M=0.37 mM for 3'-CMP K_M=2.49 mM for pNPP K_M=0.02 mM for polyphosphate V_max=10.0 µmol/min/mg enzyme with 5'-AMP as substrate V_max=22.4 µmol/min/mg enzyme with 5'-GMP as substrate V_max=16.4 µmol/min/mg enzyme with 5'-dGMP as substrate V_max=20.1 µmol/min/mg enzyme with 3'-AMP as substrate V_max=12.1 µmol/min/mg enzyme with 3'-CMP as substrate V_max=7.24 µmol/min/mg enzyme with pNPP as substrate V_max=0.10 µmol/min/mg enzyme with polyphosphate as substrate pH dependence: Optimum pH is 7.0-7.2 for nucleotidase activity.

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Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cobalt Magnesium Manganese Metal-binding Nickel Nucleotide-binding Zinc
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 cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW exopolyphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

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

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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_0000111809

Sites

Metal binding

Divalent metal cation By similarity

Metal binding

Divalent metal cation By similarity

Metal binding

Divalent metal cation By similarity

Metal binding

Divalent metal cation By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A840-1 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 33A7CD0AEE13C3DB
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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

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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: 7928962] [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: 9278503] [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: 16738553] [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: 15489502] [Abstract] Cited for: FUNCTION, CHARACTERIZATION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

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Cross-references

Sequence databases
	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	AP_003311.1. NP_417224.1.
3D structure databases
HSSP	HSSP built from PDB template 1J9L based on UniProtKB P96112.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A840. 3 interactions.
Genome annotation databases
GeneID	947211.
GenomeReviews	Gene locus JW2714 in contig AP009048_GR. Gene locus b2744 in contig U00096_GR.
KEGG	ecj:JW2714. eco:b2744.
Organism-specific databases
EchoBASE	EB1764.
EcoGene	EG11817. surE.
CMR	Search...
Phylogenomic databases
HOGENOM	P0A840.
OMA	P0A840. SINIPIK.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11817-MON. MetaCyc:EG11817-MON.
BRENDA	3.1.3.5. 246. 3.1.3.6. 246. 3.6.1.11. 246.
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...

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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:	June 16, 2009
This is version 34 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)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents