Q1RIB7 (HSLU_RICBR) 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:	RBE_0816

Organism

Rickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]

Taxonomic identifier

336407 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › belli group › Rickettsia bellii

Protein attributes

Sequence length	452 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 – 452	452	ATP-dependent protease ATPase subunit HslU HAMAP-Rule MF_00249		PRO_0000277980
Regions
	Nucleotide binding	73 – 78	6	ATP By similarity
Sites
	Binding site	31	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	263	1	ATP By similarity
	Binding site	330	1	ATP By similarity
	Binding site	402	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1RIB7 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 59DE8AA2EDCA649D	FASTA	452	49,865
	10 20 30 40 50 60 MKSTKTTNTN KKDPMGLTPS QIVNELNRFI VGQEKAKKAV AIALRNRGRR KRVEGNLRNE 70 80 90 100 110 120 IVPKNILMIG STGVGKTEIA RRLAKLTNSP FYKIEATKFT EVGYVGRDVE SIIRDLVEIA 130 140 150 160 170 180 VNTQKTIAKT EVDINAREKA IERVLESLVG KTSSSKTREK FQEKILSGEL DDTEIEISVA 190 200 210 220 230 240 DTAPVGGGSF EIPGMPGASM GVLNLGDMIG RAFGTTKTKT KKMLVKEAMS IILSEESEKL 250 260 270 280 290 300 IDQEKIIQQA INLVENDGIV FIDEIDKIAS VANSGAKNSE ISREGVQKDL LPLIEGTTVN 310 320 330 340 350 360 TKYGPVKTDH ILFIASGAFH IAKPSDLLPE LQGRLPIRVE LNSLTKEDMI KILLEPETSL 370 380 390 400 410 420 IKQYSALIGT EKVELEFTNS AIEKIADYAT TVNLEIEDIG ARRLHTILEN LLEDISFRAS 430 440 450 EMQGEKISID DKFVENQLSK ILTNLDLAKF VL

References

[1]

"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens." Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D. PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RML369-C.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000087 Genomic DNA. Translation: ABE04897.1.
RefSeq	YP_537986.1. NC_007940.1.
3D structure databases
ProteinModelPortal	Q1RIB7.
SMR	Q1RIB7. Positions 17-120.
ModBase	Search...
Protein-protein interaction databases
STRING	336407.RBE_0816.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABE04897; ABE04897; RBE_0816.
GeneID	3996279.
KEGG	rbe:RBE_0816.
PATRIC	17883133. VBIRicBel102610_0930.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1220.
HOGENOM	HOG000010036.
KO	K03667.
OMA	KYGMIKT.
ProtClustDB	PRK05201.
Enzyme and pathway databases
BioCyc	RBEL336407:GJCY-838-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_RICBR

Accession

Primary (citable) accession number: Q1RIB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	May 16, 2006
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program