ID Q9I742_PSEAE PRELIMINARY; PRT; 902 AA. AC Q9I742; DT 01-MAR-2001 (TrEMBLrel. 16, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-OCT-2003 (TrEMBLrel. 25, Last annotation update) DE Probable ClpA/B-type chaperone. GN OrderedLocusNames=PA0090; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 15692 / PAO1; RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is CC involved in the recovery of the cell from heat-induced damage, in CC cooperation with dnaK, dnaJ and grpE. Acts before dnaK, in the CC processing of protein aggregates. Protein binding stimulates the CC ATPase activity; ATP hydrolysis unfolds the denatured protein CC aggregates, which probably helps expose new hydrophobic binding CC sites on the surface of clpB-bound aggregates, contributing to the CC solubilization and refolding of denatured protein aggregates by CC dnaK (By similarity). CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- DOMAIN: The N-terminal domain probably functions as a substrate- CC discriminating domain, recruiting aggregated proteins to the clpB CC hexamer and/or stabilizing bound proteins. The NBD2 domain is CC responsible for oligomerization, whereas the NBD1 domain CC stabilizes the hexamer probably in an ATP-dependent manner. The CC movement of the coiled-coil domain is essential for clpB ability CC to rescue proteins from an aggregated state, probably by pulling CC apart large aggregated proteins, which are bound between the CC coiled-coils motifs of adjacent clpB subunits in the functional CC hexamer (By similarity). 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; AE004447; AAG03480.1; -. DR PIR; G83635; G83635. DR HSSP; P03815; 1JBK. DR GO; GO:0005524; F:ATP binding; IEA. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA. DR GO; GO:0000166; F:nucleotide binding; IEA. DR GO; GO:0005515; F:protein binding; IEA. DR GO; GO:0019538; P:protein metabolism; IEA. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR001270; Chaprnin_clpA/B. DR InterPro; IPR004176; Clp_N. DR Pfam; PF00004; AAA; 1. DR Pfam; PF02861; Clp_N; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00870; CLPAB_1; 1. KW ATP-binding; Chaperone; Coiled coil; Complete proteome; Heat shock; KW Repeat. SQ SEQUENCE 902 AA; 98737 MW; DB45A33B091C0071 CRC64; MSEISRVALF GKLNSLAYKA IEAATVFCKL RGNPYVELVH WFHQILQLPD SDLHQIVRQS GIDPARLAKD LTEALDRLPR GSTSITDLSS HVEEAVERGW VYGSLMFGES QVRTGYLVIG ILKTPSLRHA LTGLSAEFAK LKVEALTERF DEYVGASPEN GLSASDGFNA GAAPGEASGA LAPSAMGKQE ALKRFTVDLT EQARSGKLDP IVGRDEEIRQ LVDILMRRRQ NNPILTGEAG VGKTAVVEGF ALRIVAGDVP PALKDVELRA LDVGLLQAGA SMKGEFEQRL RQVIEDVQSS EKPIILFIDE AHTLVGAGGA AGTGDAANLL KPALARGTLR TVAATTWAEY KKHIEKDPAL TRRFQVVQVD EPSEHKAILM MRGVASTMEK HHQVQILDEA LEAAVRLSHR YIPARQLPDK SVSLLDTACA RTAISLHAVP AEVDDSRRRI EALETELAII RRESAIGVAT AERQRNAETL LAEERERLAA LEQRWAEEKR LVDELLETRA RLRAAAEAVD AGGVPLGEGE VRLDEEQRQA LHARLAELQA QLSALQGEEP LILPTVDYQA VASVVADWTG IPVGRMARNE IETVLNLDRH LKKRIIGQDH ALEMIAKRIQ TSRAGLDNPS KPIGVFMLAG TSGVGKTETA LALAEAMYGG EQNVITINMS EFQEAHTVST LKGAPPGYIG YGEGGVLTEA VRRKPYSVVL LDEVEKAHPD VHEIFFQVFD KGVMEDGEGR VIDFKNTLIL LTTNAGTEMI ASLCADPELM PEPEAIAKSL REPLLKIFPP ALLGRLVTIP YYPLSDDMLK AISRLQLGRI KKRVEATHKV PFEFDEGVVD LIVSRCTETE SGGRMIDAIL TNTLLPDMSR EFLTRMLEGK PLAGVRISSR DNQFHYDFAE AE //