ID A0A017HGF3_9RHOB Unreviewed; 871 AA.
AC A0A017HGF3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=Lokhon_00931 {ECO:0000313|EMBL:EYD73400.1};
OS Limimaricola hongkongensis DSM 17492.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1122180 {ECO:0000313|EMBL:EYD73400.1, ECO:0000313|Proteomes:UP000025047};
RN [1] {ECO:0000313|EMBL:EYD73400.1, ECO:0000313|Proteomes:UP000025047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17492 {ECO:0000313|EMBL:EYD73400.1,
RC ECO:0000313|Proteomes:UP000025047};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) 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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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:EYD73400.1}.
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DR EMBL; APGJ01000003; EYD73400.1; -; Genomic_DNA.
DR RefSeq; WP_017927578.1; NZ_KK088649.1.
DR AlphaFoldDB; A0A017HGF3; -.
DR STRING; 1122180.Lokhon_00931; -.
DR PATRIC; fig|1122180.6.peg.924; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000025047; 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 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:UP000025047};
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 871 AA; 95948 MW; AC08EEE811E0A6FD CRC64;
MNLEKFTERS RGFIQAAQTI AMRESHQRLA PEHVLKALMD DEQGLAANLI TNSGGDAARV
REAVDAAVTR LPKVSGDAGQ TYLDQSTGRV LDEAEKIAKK AGDSFVPAER ILMALAMVKS
KAKEALDAGK VSAQSLNAAI NAVRKGRTAD SANAEEGYDA LKKYARDLTE AAEQGRIDPI
IGRDEEIRRA MQVLSRRTKN NPVLIGEPGT GKTAIAEGLA LRIIDGDVPE SLRNKRLMSL
DMGALIAGAK YRGEFEERLK AVLKEIEAAA GEIILFIDEM HTLVGAGKAD GAMDAANLIK
PALARGELHC VGATTLDEYR KYVEKDAALA RRFQPLMVEE PTEEDTISIL RGIREKYELH
HGVRISDSAL VAAAQLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDRAIL
QMQIEAEALR REDDAASKER LAKIEEELGA MTEKADAMTA KWQAERDRLE GSRTLKERLD
RARAELDIAK REGNLARAGE LSYGVIPQLE RDLKSAEESD DPLMVEEAVR PEQIAEVVER
WTGIPTSKML EGEREKLLRM EDELGRRVIG QRPAVQAVSN AVRRARAGLN DEHRPLGSFL
FLGPTGVGKT ELTKAVAEYL FDDDQAMVRI DMSEFMEKHA VARLIGAPPG YVGYDEGGVL
TEAVRRRPYQ VILFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRRVDFKQT LIVLTSNLGA
QALSQLPDGA DASGARRDVM EAVRAHFRPE FLNRLDETII FDRLGREDMS GIVEIQLARL
EKRLANRNIT LSLDDAAKAW LADEGYDPVF GARPLKRVIQ RALQDQLAEM ILAGDIRDGE
ELCISAGADG LIVGDRVSGT RRPKPEGAVL H
//
