ID A0A4Q7DMX8_9RICK Unreviewed; 860 AA.
AC A0A4Q7DMX8;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:RZI47799.1};
GN ORFNames=EDM53_00185 {ECO:0000313|EMBL:RZI47799.1};
OS Rickettsiales endosymbiont of Peranema trichophorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=2486577 {ECO:0000313|EMBL:RZI47799.1, ECO:0000313|Proteomes:UP000291274};
RN [1] {ECO:0000313|EMBL:RZI47799.1, ECO:0000313|Proteomes:UP000291274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RICK02 {ECO:0000313|EMBL:RZI47799.1};
RA Munoz-Gomez S.A., Hess S., Burger G., Lang B.F., Susko E., Slamovits C.H.,
RA Roger A.J.;
RT "An updated phylogeny of the Alphaproteobacteria reveals that the parasitic
RT Rickettsiales and Holosporales have independent origins.";
RL Submitted (NOV-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:RZI47799.1}.
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DR EMBL; SCFA01000002; RZI47799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q7DMX8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000291274; 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:UP000291274};
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 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 95580 MW; B7363A9928208AB3 CRC64;
MNLGSFTERA KTVIQQAQTS ALASNHQTFT PEHIAYALLQ EDDSLIYRLL TSCGAEPSKI
QDEVKTALDK LPKISGSGAG QLFMTPETAQ VLTESEAIAK KLGDTFVTVE RILQALVKVQ
GTVIASAFKN SKINENQIVT AIEKMRKGRA ATSQNAEDTF ESLKRYAKDI TALAATGKLD
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIVEG LALRMISGDV PDSLKNLQLF
TLDLGALIAG AKYRGEFEER LKAVLNEISS TNGMVILFID ELHTLVGAGA ADGAMDASNL
LKPALARGEL HCIGATTLDE YRQHIEKDAA LARRFQPVFI AEPSVTDTIS MLRGLKEKYE
VHHGIRISDH AIIAAANLSN RYITQRFLPD KAIDLIDEAA SRLRMQVDSK PEALDELDRK
IMQLKIEVMA LEKEDDSKSK ERLQQLKSEL ATLEGESLDL SGRWHAEKLK IHELKLNKEK
LEQAKNDLDI AQRSGNLGRA GELMYGVIPE LQKKIQETDT IRENQLLQEV ISEDDIALVV
SKWTGIPVDK MLEGEKEKLL SMEQHIKEHV VGQDAAVQSV CSAVRRARAG LADQNKPIGS
FLFLGPTGVG KTELCKAVCQ FLFDDKKAMV RIDMSEYMEK HSVARLIGAP PGYVGYDQGG
ILTESVRRRP YQVILFDEIE KAHSDVFNVL LQVLDEGRLT DSHGRTVDFK NTVIILTSNL
GAEHIAALPE GNTVEQVRDK VMNIVKHSFK PEFLNRLDEI IIFDRLNRDN MGGIVDIQLQ
SLVELLAERK MELIVDKSAK EWLAQKGYDT VYGARPLKRV IQEYIQNPVA EQMLSGHYKE
GCKICITAKN DVLQFESYIS
//