Q9Z617 (HSLU_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent protease ATPase subunit HslU

Alternative name(s):
Unfoldase HslU

Gene names

Name:	hslU
Ordered Locus Names:	BUsg_558

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis By similarity. HAMAP-Rule MF_00249
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.
Sequence similarities	Belongs to the ClpX chaperone family. HslU subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC protein unfolding Inferred from electronic annotation. Source: HAMAP
Cellular_component	HslUV protease complex Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP ATPase activity Inferred from electronic annotation. Source: HAMAP peptidase activity, acting on L-amino acid peptides Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 443	443	ATP-dependent protease ATPase subunit HslU HAMAP-Rule MF_00249		PRO_0000160487
Regions
	Nucleotide binding	60 – 65	6	ATP By similarity
Sites
	Binding site	18	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	256	1	ATP By similarity
	Binding site	321	1	ATP By similarity
	Binding site	393	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Z617 [UniParc]. Last modified August 30, 2002. Version 2. Checksum: 914E269263FB8DB1	FASTA	443	50,030
	10 20 30 40 50 60 MSEMTPPQIV SELNKFIIGQ EQAKKAVAIA LRNRWRRMQL NNELRHEITP KNILMIGPTG 70 80 90 100 110 120 VGKTEIARRL AKLANSPFIK VEATKFTEVG YVGKEVDSII RDLTDAAIKM IRVKNIEKNK 130 140 150 160 170 180 LRVEEIVEER ILDVLVPRPK NNWTENEKNE SLLNTLQVFR KKLREGILDE KEIEINVLAS 190 200 210 220 230 240 TMGVEIMAPP GMEELTSQLQ SLFQNLGGHK KNTRRLKIKD AVLLLKEEEA AKLINQEEIK 250 260 270 280 290 300 KEAINAVEQN GIVFVDEIDK ICKRRDSSGP DVSREGVQRD LLPLVEGCTV STKYGMVKTD 310 320 330 340 350 360 HILFIASGAF QTSTPSDLIP ELQGRLPIKV ELQPLTINDF EKILTEPTAS ITAQYKALMK 370 380 390 400 410 420 TEGVCINFTK EGIRNIAEAA WKVNESMENI GARRLHTILE KLMEDISFNA CDNVGKTIEI 430 440 NSEYVGKHLD QLISNEDLGR FIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.
[2]	"Buchnera plasmid-associated trpEG probably originated from a chromosomal location between hslU and fpr." Clark M.A., Baumann P., Moran M.A. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-443.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM68096.1. AF108665 Genomic DNA. Translation: AAD19633.1.
RefSeq	NP_660885.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q9Z617.
SMR	Q9Z617. Positions 1-443.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg558.
Proteomic databases
PRIDE	Q9Z617.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM68096; AAM68096; BUsg_558.
GeneID	1005633.
KEGG	bas:BUsg558.
PATRIC	21248002. VBIBucAph100086_0592.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1220.
KO	K03667.
OMA	KYGMIKT.
ProtClustDB	PRK05201.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-598-MONOMER.
Family and domain databases
HAMAP	MF_00249. HslU.
InterPro	IPR003593. AAA+_ATPase. IPR013093. ATPase_AAA-2. IPR003959. ATPase_AAA_core. IPR019489. Clp_ATPase_C. IPR004491. HslU. [Graphical view]
PANTHER	PTHR11262:SF3. PTHR11262:SF3. 1 hit.
Pfam	PF00004. AAA. 1 hit. PF07724. AAA_2. 1 hit. PF10431. ClpB_D2-small. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. SM01086. ClpB_D2-small. 1 hit. [Graphical view]
TIGRFAMs	TIGR00390. hslU. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HSLU_BUCAP

Accession

Primary (citable) accession number: Q9Z617

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 30, 2002
Last modified:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program