ID Q48NI5_PSE14 Unreviewed; 854 AA.
AC Q48NI5;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB2 {ECO:0000313|EMBL:AAZ35973.1};
GN Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=PSPPH_0742 {ECO:0000313|EMBL:AAZ35973.1};
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ35973.1, ECO:0000313|Proteomes:UP000000551};
RN [1] {ECO:0000313|EMBL:AAZ35973.1, ECO:0000313|Proteomes:UP000000551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551};
RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., Creasy T.,
RA Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H.,
RA Feldblyum T., White O., Fraser C.M., Chatterjee A.K., Cartinhour S.,
RA Schneider D.J., Mansfield J., Collmer A., Buell C.R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP000058; AAZ35973.1; -; Genomic_DNA.
DR RefSeq; WP_004663469.1; NC_005773.3.
DR AlphaFoldDB; Q48NI5; -.
DR GeneID; 69857791; -.
DR KEGG; psp:PSPPH_0742; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_6; -.
DR Proteomes; UP000000551; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 854 AA; 95190 MW; 18092F19CFC4E673 CRC64;
MRIDRLTSKL QLALSDSQSL AVGLDHPAIE PAHLMQALLE QQGGSIKPLL LQVGFDINSL
RKELSAELDR LPKIQNPTGD VNMSQDLARL LNQADRLAQQ KGDQFISSEL VLLAAMDENS
KLGKLLLGQG VSKKALENAI NNLRGEGAVN DPNVEESRQA LDKYTVDLTK RAEEGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIINGEVPD GLRGKRLLSL
DMGALIAGAK YRGEFEERLK SLLNELSKQE GQIILFIDEL HTMVGAGKGE GSMDAGNMLK
PALARGELHC VGATTLNEYR QYIEKDAALE RRFQKVLVDE PSEEDTIAIL RGLKERYEVH
HKVAITDGAI IAAAKLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE VLDRLERRLI
QLKVEAQALK KEKDEAAIKR LEKLQEEVVR LEKEYADLEE IWTSEKAEVT GSAQIQQKIE
QSRQELEAAR RRGDLNRMAE LQYGIIPDLE RSLQMVDQHG KPENQLLRSK VTEEEIAEVV
SKWTGIPVSK MLEGEREKLL RMETLLHNRV IGQEEAVVAV SNAVRRSRAG LSDPNRPSGS
FMFLGPTGVG KTELCKALAE FLFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRKP YSLILLDEVE KAHSDVFNIL LQVLEDGRLT DSHGRTVDFR NTVIVMTSNL
GSAQIQELVG DREAQRAAVM DAVGTHFRPE FVNRIDEVVI FEPLARDQIA GITDIQLGRL
RKRLAERELA LTLSPEALDK LIAVGYDPVY GARPLKRAIQ RWIENPLAQM ILSGSFMPGT
TITGKVVDDE IVFA
//
