HSLU_BARHE
ID HSLU_BARHE Reviewed; 436 AA.
AC Q6G5G0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000255|HAMAP-Rule:MF_00249};
DE AltName: Full=Unfoldase HslU {ECO:0000255|HAMAP-Rule:MF_00249};
GN Name=hslU {ECO:0000255|HAMAP-Rule:MF_00249}; OrderedLocusNames=BH02080;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; this
CC subunit has chaperone activity. The binding of ATP and its subsequent
CC hydrolysis by HslU are essential for unfolding of protein substrates
CC subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of
CC its protein substrates and unfolds these before they are guided to HslV
CC for hydrolysis. {ECO:0000255|HAMAP-Rule:MF_00249}.
CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on each
CC side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV
CC complex is dependent on binding of ATP. {ECO:0000255|HAMAP-
CC Rule:MF_00249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00249}.
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DR EMBL; BX897699; CAF27020.1; -; Genomic_DNA.
DR RefSeq; WP_011180159.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q6G5G0; -.
DR SMR; Q6G5G0; -.
DR STRING; 283166.BH02080; -.
DR PaxDb; Q6G5G0; -.
DR PRIDE; Q6G5G0; -.
DR EnsemblBacteria; CAF27020; CAF27020; BH02080.
DR GeneID; 64156509; -.
DR KEGG; bhe:BH02080; -.
DR eggNOG; COG1220; Bacteria.
DR OMA; KYGMIKT; -.
DR Proteomes; UP000000421; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00249; HslU; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004491; HslU.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF3; PTHR48102:SF3; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00390; hslU; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding.
FT CHAIN 1..436
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_0000160477"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 61..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ SEQUENCE 436 AA; 48298 MW; DE49B7B979585402 CRC64;
MCVVFSPRET VSELDRFIIG QSDAKRSVAI ALRNRWRRQQ LDGPMRDEVM PKNILMIGPT
GVGKTGIARR LAKLAGAPFV KVEATKFTEV GYVGRDVEQI IRDLVEIAIS LVREKKRDEV
KVKAHINAEE RVLDALVGKT ASPATRESFR KKLRDGELDE KEIEIEVSDN NSNSTSTFDI
PGMPGAQMGI MNLSEIFGKM GNRTKVRKTT VKDAFKPLID DESEKLLDQD QIIQEALRVA
ENDGIVFIDE IDKIATRDGG ASAAVSREGV QRDLLPLVEG TTIATKYGQI KTDHILFIAS
GAFHVSKPSD LLPELQGRLP IRVELNPLTR EDLRRILTEP EASLIKQYIA LMATEEVHLE
ITDDAIDALA DIAVDLNARI ENIGARRLQT VMERVLDEIS FTAPDKAGTS FKVDAAYVKK
SIGDLAADVD LSRFIL