ID A0A372IFX9_9RHOB Unreviewed; 872 AA.
AC A0A372IFX9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:RFU13846.1};
GN ORFNames=DZD18_05770 {ECO:0000313|EMBL:RFU13846.1};
OS Rhodobacteraceae bacterium W635.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2303578 {ECO:0000313|EMBL:RFU13846.1, ECO:0000313|Proteomes:UP000264655};
RN [1] {ECO:0000313|EMBL:RFU13846.1, ECO:0000313|Proteomes:UP000264655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W635 {ECO:0000313|EMBL:RFU13846.1,
RC ECO:0000313|Proteomes:UP000264655};
RA Hou X.J.;
RT "Ayaqqumibacter halotolerans gen. nov., sp. nov., isolated from a saline
RT lake in Xinjiang province, China.";
RL Submitted (AUG-2018) 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:RFU13846.1}.
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DR EMBL; QVQC01000029; RFU13846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372IFX9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000264655; 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:UP000264655};
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..499
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 95758 MW; FCEAA555190BC6A6 CRC64;
MNLEKFTDRA RGFLQTAQTI AQREDHQKLV PEHLLKALLD DDQGMAATLI TRAGGDAGRV
AESLELSLAK LPKVTGDAGQ LYMDGQTAKV LGEAEKLATK AGDSFVAVER LLTALAMVKS
GAKDALDKGA VNAQALNTAI DDLRKGRTAD SAGAEDSYDA LKKYARDLTE AAREGKIDPI
IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIINGDVPE SLRNKTLMAL
DMGSLIAGAK YRGEFEERLK AVLAEITDAA GEIILFIDEM HTLVGAGKTD GAMDAANLIK
PALARGELHC VGATTLDEYR KYVEKDAALA RRFQPLMVAE PTVEDTVSIL RGIKEKYELH
HGVRVSDAAL VAAAQLSNRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDRDIL
QKQIEAEALK KEDDAASKDR LEKLQKDLSE LQQKSAEMTA QWQAERDKLE GARTLKEKLD
QARAELDQAK RQGDLARAGE LSYGIIPKLE KDLSEAEARD DSDLMVEEAV RPEQIASVVE
RWTGIPMSKM LEGEREKLLR MEEEIGKRVI GQKTAVRAVS NAVRRARAGL QDENRPLGSF
LMLGPTGVGK TELTKALAEY LFDDDQAMVR IDMSEFMEKH SVARLIGAPP GYVGYDEGGV
LTEAVRRRPY QVVLFDEVEK AHPDVFNVLL QVLDDGVLTD GHGRTVDFKQ TLIVLTSNLG
AQALSQLPEG ADSSDAKREV MDAVRAHFRP EFLNRLDETI IFDRLSRDDM GAIVEIQLRL
LEKRLADRKI RLELDADALQ WLADEGYDPV FGARPLKRVI QSALQNQLAE MILAGEVKDG
DTVHVSAGAD GLLVGDRVSA SNRPKPEDAV VH
//