ID I4C7U2_DESTA Unreviewed; 863 AA.
AC I4C7U2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Desti_2964 {ECO:0000313|EMBL:AFM25633.1};
OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC Desulfomonilaceae; Desulfomonile.
OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM25633.1, ECO:0000313|Proteomes:UP000006055};
RN [1] {ECO:0000313|Proteomes:UP000006055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC {ECO:0000313|Proteomes:UP000006055};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003360; AFM25633.1; -; Genomic_DNA.
DR RefSeq; WP_014810770.1; NC_018025.1.
DR AlphaFoldDB; I4C7U2; -.
DR STRING; 706587.Desti_2964; -.
DR KEGG; dti:Desti_2964; -.
DR PATRIC; fig|706587.4.peg.3370; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000006055; 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 Reference proteome {ECO:0000313|Proteomes:UP000006055};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 85..112
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 96625 MW; 23B9AC1BD8D76159 CRC64;
MRADKFTLKS QEALELAQNT AANRGNPQVE VEHLLLALLS DEEGLPVEIV KKLGTDLDRI
RNETLKAVER LPTQSGTTTA DRYFSNQLRE VLEKAFKEME QLKDEYLSVE HMLIAIAESS
GTQAGKILTS RGVTKDKIYV VLTDIRGTQR VTDQSPEEKY QALKRFTKDL TELARKGKLD
PVIGRDEEIR RIIQVLSRRT KNNPVLIGDP GVGKTAIVEG LASRIISGDI PESLKGKRVL
ALDLGQLIAG AKYRGEFEDR LKAVLKEITG ASGEIILFID EMHTLVGAGA AEGAVDASNM
LKPPLARGEL RAIGATTVEE YRKYIEKDKA LERRFQPIYV AEPSVEDTIS ILRGLKERYE
LHHGVRIQDA AIIAAATLSH RYITDRFLPD KAVDLIDEAS SRLRIEIDSM PTEIDTIERR
IIQLQIEEQA LTKESDPASK ERLQKVKFEI ERLADESNAL KEEWQKEKKI ISGIRELKER
LERAKVDAVK AEREGNLSKA AELKYGMIIS LEKDIAAKNE ELENLQKGGG LLKEEVGPED
VAEVVAKWTG IPVSKMLEGE LDKLLKMEER LSQRVVGQPE AIVAVSDAVR RARSGLHDPN
RPIGSFIFLG PTGVGKTELA RALAEFLFDD EQAIVRVDMS EYMERHSVAR LIGAPPGYVG
YEEGGYLTEA VRRRPYSVVL FDEIEKAHPE VFNALLQILD DGRLTDGKGR TVDFKNTIII
MTSNIGSSEI RELAGVSEER MRQRVMDALR AHFKPEFLNR LDDIIIFHAL TKDQIKKIVD
IQMNRLNKRL AESKLHLVLD DGARELLSSE GFDPAYGARP LKRAIQRLIE NRLSLDLLKG
RFQPGDTIVA KVDGNQLAFD KAA
//
