Skip Header

Contribute Send feedback
Read comments (?) or add your own

P43772 (HSLV_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent protease subunit HslV
EC=3.4.25.2
Gene names
Name:hslV
Ordered Locus Names:HI_0496
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. HAMAP MF_00248

Catalytic activity

ATP-dependent cleavage of peptide bonds with broad specificity. HAMAP MF_00248

Enzyme regulation

Allosterically activated by HslU binding. Ref.5

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.

Subcellular location

Cytoplasm By similarity HAMAP MF_00248.

Sequence similarities

Belongs to the peptidase T1B family. HslV subfamily.

Biophysicochemical properties

Kinetic parameters:

Arc-H(6)-SulA(CT) is a construct consisting of the Arc repressor protein fused to 6 His residues and the 11 carboxy terminal residues of SulA.

KM=2.3 µM for Arc-H(6)-SulA(CT) Ref.2

Binary interactions

With

Entry

#Exp.

IntAct

Notes

hslUP437734EBI-1030290,EBI-1030296

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 175174ATP-dependent protease subunit HslV HAMAP MF_00248
PRO_0000148111

Sites

Active site21
Metal binding1581Sodium; via carbonyl oxygen
Metal binding1611Sodium; via carbonyl oxygen
Metal binding1641Sodium; via carbonyl oxygen

Secondary structure

1 .................................. 175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43772 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CEA1C77B7AB2724C

FASTA17519,012
        10         20         30         40         50         60 
MTTIVSVRRN GQVVVGGDGQ VSLGNTVMKG NARKVRRLYN GKVLAGFAGG TADAFTLFEL 

        70         80         90        100        110        120 
FERKLEMHQG HLLKSAVELA KDWRTDRALR KLEAMLIVAD EKESLIITGI GDVVQPEEDQ 

       130        140        150        160        170 
ILAIGSGGNY ALSAARALVE NTELSAHEIV EKSLRIAGDI CVFTNTNFTI EELPN

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed: 7542800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]"Kinetics of protein substrate degradation by HslUV."
Kwon A.-R., Trame C.B., McKay D.B.
J. Struct. Biol. 146:141-147(2004) [PubMed: 15037245] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[3]"Crystal and solution structures of an HslUV protease-chaperone complex."
Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., McKay D.B.
Cell 103:633-643(2000) [PubMed: 11106733] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS) OF 2-175 IN COMPLEX WITH HSLU.
[4]"Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site."
Sousa M.C., McKay D.B.
Acta Crystallogr. D 57:1950-1954(2001) [PubMed: 11717526] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH POTASSIUM OR SODIUM.
[5]"Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU."
Sousa M.C., Kessler B.M., Overkleeft H.S., McKay D.B.
J. Mol. Biol. 318:779-785(2002) [PubMed: 12054822] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLU AND INHIBITOR, ENZYME REGULATION.
[6]"Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome."
Kwon A.-R., Kessler B.M., Overkleeft H.S., McKay D.B.
J. Mol. Biol. 330:185-195(2003) [PubMed: 12823960] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLU; MAGNESIUM; ADP AND INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC22153.1.
PIRC64072.
RefSeqNP_438654.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G3IX-ray3.41G/H/I/J/K/L/M/N/O/P/Q/R2-175[»]
1G3KX-ray1.90A/B/C2-175[»]
1JJWX-ray1.90A/B/C2-175[»]
1KYIX-ray3.10G/H/I/J/K/L/M/N/O/P/Q/R2-174[»]
1OFHX-ray2.50G/H/I/L/M/N2-174[»]
1OFIX-ray3.20G/H/I/L/M/N2-174[»]
ProteinModelPortalP43772.
SMRP43772. Positions 2-174.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6176N.
IntActP43772. 1 interaction.

Protein family/group databases

MEROPST01.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID949571.
GenomeReviewsGene locus HI_0496 in contig L42023_GR.
KEGGhin:HI0496.
PATRIC20189543. VBIHaeInf48452_0514.
TIGRHI_0496.

Phylogenomic databases

HOGENOMHBG288822.
OMAWRTDKYL.
ProtClustDBPRK05456.

Enzyme and pathway databases

BioCycHINF71421:HI_0496-MONOMER.

Family and domain databases

HAMAPMF_00248. HslV.
[Tree]
InterProIPR022281. ATP-dep_Prtase_HsIV_su.
IPR001353. Proteasome_sua/b.
[Graphical view]
KOK01419.
PANTHERPTHR11599:SF38. PTHR11599:SF38. 1 hit.
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
TIGRFAMsTIGR03692. ATP_dep_HslV. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHSLV_HAEIN
AccessionPrimary (citable) accession number: P43772
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents