P0A7C0 (HSLV_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent protease subunit HslV
EC=3.4.25.2

Alternative name(s):
Heat shock protein HslV

Gene names

Name:	hslV
Ordered Locus Names:	Z5479, ECs4859

Organism

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

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery By similarity. HAMAP-Rule MF_00248
Catalytic activity	ATP-dependent cleavage of peptide bonds with broad specificity. HAMAP-Rule MF_00248
Enzyme regulation	Allosterically activated by HslU binding By similarity. HAMAP-Rule MF_00248
Subunit structure	A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP By similarity.
Subcellular location	Cytoplasm By similarity.
Induction	By heat shock By similarity.
Sequence similarities	Belongs to the peptidase T1B family. HslV subfamily.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	Metal-binding Sodium
Molecular function	Hydrolase Protease Threonine protease
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological_process	proteolysis involved in cellular protein catabolic process Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	HslUV protease complex Inferred from electronic annotation. Source: HAMAP proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW threonine-type endopeptidase activity 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 176	175	ATP-dependent protease subunit HslV HAMAP-Rule MF_00248		PRO_0000148106
Sites
	Active site	2	1	By similarity
	Metal binding	157	1	Sodium; via carbonyl oxygen By similarity
	Metal binding	160	1	Sodium; via carbonyl oxygen By similarity
	Metal binding	163	1	Sodium; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A7C0 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 3B35E01F51486965	FASTA	176	19,093
	10 20 30 40 50 60 MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG TADAFTLFEL 70 80 90 100 110 120 FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD ETASLIITGN GDVVQPENDL 130 140 150 160 170 IAIGSGGPYA QAAARALLEN TELSAREIAE KALDIAGDIC IYTNHFHTIE ELSYKA

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG59127.1. BA000007 Genomic DNA. Translation: BAB38282.1.
PIR	C86083. C91236.
RefSeq	NP_290563.1. NC_002655.2. NP_312886.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0A7C0.
SMR	P0A7C0. Positions 2-175.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1218920.
STRING	155864.Z5479.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG59127; AAG59127; Z5479. BAB38282; BAB38282; BAB38282.
GeneID	915032. 960205.
KEGG	ece:Z5479. ecs:ECs4859.
PATRIC	18359379. VBIEscCol44059_4839.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG5405.
HOGENOM	HOG000064533.
KO	K01419.
OMA	KDWRTDK.
ProtClustDB	PRK05456.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-4849-MONOMER.
Family and domain databases
HAMAP	MF_00248. HslV.
InterPro	IPR022281. ATP-dep_Prtase_HsIV_su. IPR001353. Proteasome_sua/b. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
TIGRFAMs	TIGR03692. ATP_dep_HslV. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HSLV_ECO57

Accession

Primary (citable) accession number: P0A7C0
Secondary accession number(s): P31059, P97542

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program