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).
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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
//