ID HSLU_LEPIN Reviewed; 479 AA. AC Q8F3Q5; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 01-OCT-2014, entry version 77. 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}; GN OrderedLocusNames=LA_2345; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai OS (strain 56601). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=189518; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601; RX PubMed=12712204; DOI=10.1038/nature01597; RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., RA Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., RA Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., RA Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., RA Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., RA Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., RA Xu J.-G., Zhao G.-P.; RT "Unique physiological and pathogenic features of Leptospira RT interrogans revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). CC -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; CC this subunit has chaperone activity. The binding of ATP and its CC subsequent hydrolysis by HslU are essential for unfolding of CC protein substrates subsequently hydrolyzed by HslV. HslU CC recognizes the N-terminal part of its protein substrates and CC unfolds these before they are guided to HslV for hydrolysis. CC {ECO:0000255|HAMAP-Rule:MF_00249}. CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on CC each side by a ring-shaped HslU homohexamer. The assembly of the CC HslU/HslV complex is dependent on binding of ATP. CC {ECO:0000255|HAMAP-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}. 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; AE010300; AAN49544.1; -; Genomic_DNA. DR RefSeq; NP_712526.1; NC_004342.2. DR ProteinModelPortal; Q8F3Q5; -. DR SMR; Q8F3Q5; 17-147. DR STRING; 189518.LA2345; -. DR PaxDb; Q8F3Q5; -. DR EnsemblBacteria; AAN49544; AAN49544; LA_2345. DR GeneID; 1151688; -. DR KEGG; lil:LA_2345; -. DR PATRIC; 22385522; VBILepInt91350_2329. DR eggNOG; COG1220; -. DR HOGENOM; HOG000010036; -. DR KO; K03667; -. DR OMA; PVGVEIM; -. DR OrthoDB; EOG6NPM7G; -. DR BioCyc; LINT189518:GJBB-1909-MONOMER; -. DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro. DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-HAMAP. 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; IPR011704; ATPase_dyneun-rel_AAA. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004491; HslU. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11262:SF3; PTHR11262:SF3; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF07728; AAA_5; 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; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 479 ATP-dependent protease ATPase subunit FT HslU. FT /FTId=PRO_0000160519. FT NP_BIND 74 79 ATP. {ECO:0000255|HAMAP-Rule:MF_00249}. FT BINDING 32 32 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00249}. FT BINDING 290 290 ATP. {ECO:0000255|HAMAP-Rule:MF_00249}. FT BINDING 355 355 ATP. {ECO:0000255|HAMAP-Rule:MF_00249}. FT BINDING 427 427 ATP. {ECO:0000255|HAMAP-Rule:MF_00249}. SQ SEQUENCE 479 AA; 53988 MW; 51D0B2DDBE94DA9B CRC64; MANHPIDQEL TSPAEEELTP REIVAKLDEH IISQKNAKKA VAIALRNRTR RKKLDPEMRE EIYPKNIIMI GPTGVGKTEI ARRLSKLCGA PFLKVEATKY TEVGYVGRDV ESMIRDLAVI SMNLVKQEFR TKVEETAKQK AEEALLDILL PFPGENKHGS GQITGFATSS TLADEEDRKT HFLETREFMR KKLKTGKLDD QEVELDLPNP SVSQVPMLQV FGAGNLDDLD NQLQNVLGDI LPKKNKKRKL KIPEALKALE ESEAEKLLDP DKVQREALRR VEEMGIIFLD EIDKIAGREG KSGADVSREG VQRDLLPIVE GATVNTKIGP VKTDHILFIA AGAFHMTKPS DLIPELQGRF PIRVELEKLS REDFEKILTA PCSSLTRQYE ALLSTDGIQL EFSLDGIQEI ARIAYDMNEK HENIGARRLN TILERLLEEV SFEGPDLPES QRKVRIDGKY VTDRLQGVIQ NKDLSQYIL //