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Database: UniProt
Entry: A0A5C4MQN4_9RHOB
LinkDB: A0A5C4MQN4_9RHOB
Original site: A0A5C4MQN4_9RHOB 
ID   A0A5C4MQN4_9RHOB        Unreviewed;       874 AA.
AC   A0A5C4MQN4;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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:TNC47871.1};
GN   ORFNames=FHG66_15475 {ECO:0000313|EMBL:TNC47871.1};
OS   Rubellimicrobium rubrum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=2585369 {ECO:0000313|EMBL:TNC47871.1, ECO:0000313|Proteomes:UP000305887};
RN   [1] {ECO:0000313|EMBL:TNC47871.1, ECO:0000313|Proteomes:UP000305887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 131921 {ECO:0000313|EMBL:TNC47871.1,
RC   ECO:0000313|Proteomes:UP000305887};
RA   Jiang L.;
RT   "YIM 131921 draft genome.";
RL   Submitted (JUN-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:TNC47871.1}.
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DR   EMBL; VDFU01000021; TNC47871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C4MQN4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000305887; 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};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000305887};
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   REGION          431..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  96432 MW;  ACC71BDEC2595DA3 CRC64;
     MNLEKFTERS RGFLQAAQTI AIREQNQRVL PEHLLKALMD DDQGLAANLI DRSGGSSARV
     REAVDAAVAR QPKVSGDAGQ AYVDSSLVRV LDEAEKVATK AGDSFVPVER MLMALAMVKS
     KAQEALDAGA VTAQKLNAAI NDVRKGRTAD TASAEEGYDA LRKYARDLTE AARDGKIDPI
     IGRDEEIRRS MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLRNKTLMAL
     DMGSLIAGAK YRGEFEERLK AVLKEIEAAA GEVIVFIDEM HTLVGAGKAD GAMDAANLIK
     PALARGELHC IGATTLDEYR KHVEKDAALA RRFQPIMVEE PTVEDTISIL RGIKEKYELH
     HGVRISDSAL VAAAQLSHRY ITDRFLPDKA IDLVDEAASR LRMEIDSKPE ELDQLDRQLL
     QLQIEAEALK KEDDDASKDR LSRLEKEMSE VQERSAAMTA KWQAERATLE SARFVKERLE
     DARAQLDRAK REGNLAEAGR LAYGEIPQLE RELAEAETQG DGLMVEEAVR PEQIAEVVER
     WTGIPTSRML EGERDKLLRM EEALGKRVVG QRAAVEAVSR AVRRARAGLN DEGRPLGSFL
     FLGPTGVGKT ELTKALAEFL FDDDTAMVRI DMSEFMEKHA VSRLIGAPPG YVGYDEGGVL
     TEAVRRRPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGMLTDG QGRTVDFKQT IIVLTSNLGA
     RALSELPEGS DATLAKREVM EAVRTHFRPE FLNRLDEQII FDRLDRSDMT GIVEIQLKRL
     EKRLAARKIR LDLDQGAKQW LADEGYDPVF GARPLKRVIQ RALQDQLAEM ILAGEVRDDE
     TVTVTAGPDG LIVGNRVASG SGARTDRPMD AVVH
//
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