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 19-JAN-2010, entry version 45. DE RecName: Full=ATP-dependent hsl protease ATP-binding subunit hslU; GN Name=hslU; OrderedLocusNames=LA_2345; OS Leptospira interrogans. OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=173; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601 / Serogroup Icterohaemorrhagiae / Serovar lai; RX MEDLINE=22598143; 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: Chaperone subunit of a proteasome-like degradation CC complex (By similarity). CC -!- SUBUNIT: A double ring-shaped homohexamer of hslV is capped on CC each side by a ring-shaped hslU homohexamer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the clpX chaperone family. HslU subfamily. 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; -. DR SMR; Q8F3Q5; 17-479. DR GeneID; 1151688; -. DR GenomeReviews; AE010300_GR; LA_2345. DR KEGG; lil:LA2345; -. DR NMPDR; fig|189518.1.peg.2345; -. DR HOGENOM; HBG745965; -. DR OMA; GRFPLRV; -. DR BioCyc; LINT189518:LA2345-MONOMER; -. DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0070011; F:peptidase activity, acting on L-amino acid ...; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR HAMAP; MF_00249; HslU; 1; -. DR InterPro; IPR003593; ATPase_AAA+_core. DR InterPro; IPR013093; ATPase_AAA-2. DR InterPro; IPR011704; ATPase_AAA-5. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004491; HslU. DR PANTHER; PTHR11262:SF3; HslU; 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. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding. FT CHAIN 1 479 ATP-dependent hsl protease ATP-binding FT subunit hslU. FT /FTId=PRO_0000160519. FT NP_BIND 71 78 ATP (Potential). 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 //