ID A0AAF1DAR3_9NEIS Unreviewed; 440 AA. AC A0AAF1DAR3; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 02-OCT-2024, entry version 3. DE RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000256|HAMAP-Rule:MF_00249}; DE AltName: Full=Unfoldase HslU {ECO:0000256|HAMAP-Rule:MF_00249}; GN Name=hslU {ECO:0000256|HAMAP-Rule:MF_00249, GN ECO:0000313|EMBL:QED92908.1}; GN ORFNames=EZJ17_02330 {ECO:0000313|EMBL:QED92908.1}; OS Eikenella exigua. OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Eikenella. OX NCBI_TaxID=2528037 {ECO:0000313|EMBL:QED92908.1}; RN [1] {ECO:0000313|EMBL:QED92908.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PXX {ECO:0000313|EMBL:QED92908.1}; RX PubMed=31693476; RA Stormo K.A., Nygaard R.M., Bruvold T.S., Dimmen G., Lindemann P.C., RA Jordal S., Kommedal O.; RT "Eikenella exigua sp. nov., isolated from brain abscess and blood."; RL Int. J. Syst. Evol. Microbiol. 70:1478-1488(2020). 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:0000256|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:0000256|HAMAP- CC Rule:MF_00249}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249}. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily. CC {ECO:0000256|ARBA:ARBA00009771, ECO:0000256|HAMAP-Rule:MF_00249}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP038018; QED92908.1; -; Genomic_DNA. DR KEGG; eex:EZJ17_02330; -. 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:UniProtKB-KW. DR GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule. DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule. DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:TreeGrafter. DR CDD; cd19498; RecA-like_HslU; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR HAMAP; MF_00249; HslU; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR050052; ATP-dep_Clp_protease_ClpX. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004491; HslU. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00390; hslU; 1. DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1. DR PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM01086; ClpB_D2-small; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00249}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00249}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249}; KW Hydrolase {ECO:0000313|EMBL:QED92908.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249}; KW Protease {ECO:0000313|EMBL:QED92908.1}. FT DOMAIN 46..332 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT DOMAIN 335..428 FT /note="Clp ATPase C-terminal" FT /evidence="ECO:0000259|SMART:SM01086" FT REGION 131..154 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249" FT BINDING 57..62 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249" FT BINDING 256 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249" FT BINDING 321 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249" FT BINDING 393 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249" SQ SEQUENCE 440 AA; 48976 MW; C3E4601D34463D69 CRC64; MTPQEIVHEL DKHIIGQQQA KKAVAVALRN RYRRSQVAEP LQSEIVPKNI LMIGPTGVGK TEIARRLARL ANAPFIKIEA TKFTEVGYVG RDVDSIVRDL MEIALKNLRE QAVRKNRARA QDAAENRVLD ALLPPPPQTG FEGEPAEPQP ESHTRKKFRE MLRQGELDDK EINIELSQAS PTSMQVMGPP GMEEFSSQLQ DMFANLSKGR TKPHKIKVAA AMKLLLDEEA AKLINEEELR EQAVHAVEQH GIVFLDEIDK IAADSNRHGG DVSRQGVQRD LLPLVEGTTV QTKYGMIKTD HILFIASGAF HLSKPSDLIP ELQGRFPIRV ELSSLTVEDF QAILTSTDAS LTKQYQALLA TDGVELDFAP DGITRLAEIA FQVNEKTENI GARRLHTVLE KLLEDVSFHA PQGTTQITAA YVDERLAEVA EQEDLARYVL //