ID A0A4R5V347_9RHOB Unreviewed; 872 AA.
AC A0A4R5V347;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:TDK46298.1};
GN ORFNames=E1832_13030 {ECO:0000313|EMBL:TDK46298.1};
OS Antarcticimicrobium luteum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Antarcticimicrobium.
OX NCBI_TaxID=2547397 {ECO:0000313|EMBL:TDK46298.1, ECO:0000313|Proteomes:UP000295301};
RN [1] {ECO:0000313|EMBL:TDK46298.1, ECO:0000313|Proteomes:UP000295301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=318-1 {ECO:0000313|EMBL:TDK46298.1,
RC ECO:0000313|Proteomes:UP000295301};
RA Kim J., Kim D.-Y., Lee S.-S.;
RT "Ruegeria lutea sp. nov., a novel strain, isolated from marine sediment,
RT the Masan Bay, South Korea.";
RL Submitted (MAR-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. 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|ARBA:ARBA00004496,
CC 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:TDK46298.1}.
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DR EMBL; SMUV01000067; TDK46298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R5V347; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000295301; 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 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..529
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 95835 MW; 6F081320E6D28BE9 CRC64;
MDLNKFTERA RGFVQAAQTI AMREEHQRLA PEHLLKALMD DDQGLASNLI QRAGGAPARV
VEALDVAINK IPKVSGDAGQ IYLDTQTAKV LDEAEKVAKK AGDSFVPVER ILMALCMVKS
PAKEALEAGA VTAQKLNEAI NDIRKGRTAD TANAEEGYDA LKKYARDLTE AAREGKIDPI
IGRDDEIRRS MQVLSRRTKN NPVLIGEPGV GKTAIAEGMA LRIINGDVPE SLKNKKLLAL
DMGALIAGAK YRGEFEERLK AILKEIEAAA GEVILFIDEM HTLVGAGKSD GAMDAANLIK
PALARGELHC IGATTLDEYR KYVEKDAALA RRFQPVMVTE PTVEDTISIL RGIKEKYELH
HGVRISDSAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDQLDRQIL
QLQIEEQALK LEDDTAARDR LETLQKDLAD LQERSAEMTA QWQAERDKLA GARDLKEQLD
RARADLEIAK REGNLAKAGE LSYGVIPQLE KQLAEAEQAE DEDMMVEEAV RPEQIAAVVE
RWTGIPTSKM LEGEREKLLR MEDELHKRVI GQDAAVRAVA NAVRRARAGL NDEGRPLGSF
LFLGPTGVGK TELTKAVANY LFDDDNAMVR IDMSEFMEKH AVARLIGAPP GYVGYDEGGV
LTEAVRRRPY QVVLFDEVEK AHPDVFNVLL QVLDDGVLTD GHGRTVDFKQ TLIVLTSNLG
SQALSQLPEG ADGAQARRDV MDAVRAHFRP EFLNRLDETI IFDRLSRDNM SAIVNIQIGL
LQKRLAGRKI ALELDEGALK WLADEGYDPV FGARPLKRVI QTALQNPLAE MLLAGDVKDG
DTLPVTAGAE GLIIGERVGA SNRPKPDDAV VH
//