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Database: UniProt
Entry: A0A4Q7DMX8_9RICK
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Original site: A0A4Q7DMX8_9RICK 
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
//
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