HSLU_BRUA2
ID HSLU_BRUA2 Reviewed; 434 AA.
AC Q2YQZ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=BAB1_2080;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ12036.1; -; Genomic_DNA.
DR RefSeq; WP_002967032.1; NZ_KN046823.1.
DR PDB; 7MHB; X-ray; 2.60 A; A/B=3-418.
DR PDBsum; 7MHB; -.
DR AlphaFoldDB; Q2YQZ4; -.
DR SMR; Q2YQZ4; -.
DR STRING; 359391.BAB1_2080; -.
DR EnsemblBacteria; CAJ12036; CAJ12036; BAB1_2080.
DR GeneID; 3788757; -.
DR KEGG; bmf:BAB1_2080; -.
DR PATRIC; fig|359391.11.peg.1314; -.
DR HOGENOM; CLU_033123_0_0_5; -.
DR OMA; KYGMIKT; -.
DR PhylomeDB; Q2YQZ4; -.
DR Proteomes; UP000002719; Chromosome I.
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; -; 1.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..434
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_1000012707"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 60..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 21..39
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 97..116
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:7MHB"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:7MHB"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 361..377
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 395..400
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:7MHB"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:7MHB"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:7MHB"
SQ SEQUENCE 434 AA; 47939 MW; 9B47F6265A033B10 CRC64;
MSNFSPREIV SELDRFIIGQ KDAKRAVAIA LRNRWRRQQL EGQMREEVMP KNILMIGPTG
VGKTEISRRL AKLAGAPFVK VEATKFTEVG YVGRDVEQII RDLVEIAITL VREKRREDVK
AKAHLNAEER VLDALVGKTA SPATRDSFRK KLRNGEMDDK EIEIEVSDSG ASPNFEIPGM
PGANIGVLNI SDMLGKAMGG RTKTRKTTVK DSYPILINDE SDKLLDQDQI VQEALRVSED
EGIVFIDEID KIAAREGGSG AGVSREGVQR DLLPLVEGTT VATKYGPVKT DHILFITSGA
FHVSKPSDLL PELQGRLPIR VELSALTRED FRRILTETEA SLIKQYIALM ETEEVKLEFS
DDAIDALADI AVDLNATVEN IGARRLQTVI EKVLDEISFT APDKAGATFI IDAAYVKEKI
GGLAKNTDLS RFIL
