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 26-FEB-2020, entry version 97. 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=LA_2345; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain OS 56601). OC Bacteria; Spirochaetes; Leptospirales; 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., Zhang Y.-X., RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F., RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.; RT "Unique physiological and pathogenic features of Leptospira interrogans RT revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). 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}. 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 RefSeq; WP_001273640.1; NC_004342.2. DR SMR; Q8F3Q5; -. DR EnsemblBacteria; AAN49544; AAN49544; LA_2345. DR GeneID; 1151688; -. DR KEGG; lil:LA_2345; -. DR PATRIC; fig|189518.3.peg.2329; -. DR eggNOG; ENOG4105C4N; Bacteria. DR eggNOG; COG1220; LUCA. DR HOGENOM; CLU_033123_0_0_12; -. DR InParanoid; Q8F3Q5; -. DR KO; K03667; -. DR OMA; KYGMIKT; -. DR BioCyc; LINT189518:G1GL4-1903-MONOMER; -. DR Proteomes; UP000001408; 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:ATPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro. DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule. 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; PTHR43815; PTHR43815; 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; Cytoplasm; Nucleotide-binding; Reference proteome. FT CHAIN 1..479 FT /note="ATP-dependent protease ATPase subunit HslU" FT /id="PRO_0000160519" FT NP_BIND 74..79 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249" FT BINDING 32 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249" FT BINDING 290 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249" FT BINDING 355 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249" FT BINDING 427 FT /note="ATP" FT /evidence="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 //