ID A0A5C8Z079_9GAMM Unreviewed; 861 AA.
AC A0A5C8Z079;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TXR51525.1};
GN ORFNames=FME95_13475 {ECO:0000313|EMBL:TXR51525.1};
OS Reinekea thalattae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Reinekea.
OX NCBI_TaxID=2593301 {ECO:0000313|EMBL:TXR51525.1, ECO:0000313|Proteomes:UP000321764};
RN [1] {ECO:0000313|EMBL:TXR51525.1, ECO:0000313|Proteomes:UP000321764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSH23 {ECO:0000313|EMBL:TXR51525.1,
RC ECO:0000313|Proteomes:UP000321764};
RA Kim I.;
RT "Reinekea sp. strain SSH23 genome sequencing and assembly.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TXR51525.1}.
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DR EMBL; VKAD01000003; TXR51525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C8Z079; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000321764; Unassembled WGS sequence.
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 104; 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 Reference proteome {ECO:0000313|Proteomes:UP000321764};
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 861 AA; 95923 MW; FB3C91A875AA7B12 CRC64;
MRIDRLTSSL QLALSDAQSV ALGNDNSFIE PVHLLLAMLN QKKTSLAALV KNANGQLSVL
RSAADQLLQS LPKVSGGDDD VHMSNDLGRV LNRADKYSQQ RNDQYISTEL VILAMLKDRS
AIAKVLAEAG LTEDNLTAAI DKLRNGESVT SAEAEDARQA LDRYTVDLTA RAEEGRLDPV
IGRDDEIRRT IQVLQRRRKN NPVLIGEPGV GKTAIVEGLA QRILNGEVPE SLKNKRVLSL
DLGALVAGAK YRGEFEERLK AVLNELGKQE GQIILFIDEL HTMVGAGKSD GAMDAGNMLK
PALSRGELHC VGATTLDEYR QYIEKDGALE RRFQKVQVSE PSEEDSIAIL RGLKERYEVH
HGVTITDGAL ISAVKFSQRY ISDRKLPDKA IDLIDEAASH IRMEIDSKPE SMDILERKLI
QLKIEAEAIK KDTSESTTQT LSKLEKQIED TENEYADLEE IWITEKAAVQ GSQHIKEQLE
QARVELEMAR RNSDLARMSE LQYGEIPELE KRLDMASQAE MMDMKLLQNK VTKESIAKVI
SRWTGIPIDK MLEGERSKLL RMEEVLHGRL IGQDEAVTAV ANAIRRSRSG LSDPKRPNGS
FLFLGPTGVG KTELCKTLAH FLFDTTESLV RVDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTETVRRKP YSVVLLDEVE KAHADVFNIL LQVLEDGRLT DGQGRTVDFR NTVIVMTSNL
GSAQIQLLAD NSDYEEMKAG VMDEVSTFFR PEFINRLDEV VVFHPLASEH IQGIAEIQLA
QLHDRLDEMS MDIRLTPEVM SLICEAGFDP VYGARPLKRA IQRKLENPLA EALLRADFDS
GDTIEAFLED GEVGFRKINQ S
//