ID A0A238LJG2_9RHOB Unreviewed; 871 AA.
AC A0A238LJG2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:SMY09030.1};
GN ORFNames=LOM8899_03191 {ECO:0000313|EMBL:SMY09030.1};
OS Flavimaricola marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Flavimaricola.
OX NCBI_TaxID=1819565 {ECO:0000313|EMBL:SMY09030.1, ECO:0000313|Proteomes:UP000201613};
RN [1] {ECO:0000313|EMBL:SMY09030.1, ECO:0000313|Proteomes:UP000201613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8899 {ECO:0000313|EMBL:SMY09030.1,
RC ECO:0000313|Proteomes:UP000201613};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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}.
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DR EMBL; FXZK01000006; SMY09030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238LJG2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000201613; 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:UP000201613};
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..439
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 95195 MW; 0DD056590D912582 CRC64;
MNLEKFTERS RGFVQAAQTI AVRESHQRLA PEHLLKALMD DDQGLASNLI NASGGDARAV
VDAVDAAVAK HAKVTGDAAQ VYVDNTTAKV LTEAEALAKK AGDSFVPVER LLMALAMVKS
KAKDALDAGK VTPQGLNAAI NDVRKGRTAD SATAEEGYDA LKKYARDLTE AAEQGKIDPI
IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIIDGDVPE SLRNKRLMAL
DMGALIAGAK YRGEFEERLK AVLNEITAAA GEIILFIDEM HTLVGAGKAD GAMDAANLIK
PALARGELHC VGATTLDEYR KYVEKDAALA RRFQPLMVEE PTVEDTVSIL RGIKEKYELH
HGVRISDSAL VAAATLSHRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDALDRQIL
QMQIEAEALK KEDDQASKDR LSKIEKDLGD MMEKADAMTA KWQAERDRLE GSRGMKEKLD
RARADLEIAK REGNLAKAGE LSYGVIPQLE KALAEADAEG DALMVEEAVR PEQIAEVVER
WTGIPTSRML EGERDKLLRM EEGLHKRVIG QNTAVRAVAN AVRRARAGLN DEGRPLGSFL
FLGPTGVGKT ELTKAVAEFL FDDENAMVRI DMSEFMEKHA VARLIGAPPG YVGYDEGGVL
TEAVRRRPYQ VILFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRTVDFKQT LIVLTSNLGA
QALSQLPDGA DASSAKRDVM DAVRAHFRPE FLNRLDETII FDRLGRADMT GIVEIQLGLL
RKRLAGRNMT LDLDEAALKW LADEGYDPVF GARPLKRVIQ RALQDQLAEM ILSGDLMDGD
SVPVTVGPEG LIVGDRLASS NRPKPDDAVV H
//
