GenomeNet

Database: UniProt
Entry: A0A399IZ79_9RHOB
LinkDB: A0A399IZ79_9RHOB
Original site: A0A399IZ79_9RHOB 
ID   A0A399IZ79_9RHOB        Unreviewed;       872 AA.
AC   A0A399IZ79;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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:RII37579.1};
GN   ORFNames=DL237_17005 {ECO:0000313|EMBL:RII37579.1};
OS   Pseudopuniceibacterium sediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudopuniceibacterium.
OX   NCBI_TaxID=2211117 {ECO:0000313|EMBL:RII37579.1, ECO:0000313|Proteomes:UP000265848};
RN   [1] {ECO:0000313|EMBL:RII37579.1, ECO:0000313|Proteomes:UP000265848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CY03 {ECO:0000313|EMBL:RII37579.1,
RC   ECO:0000313|Proteomes:UP000265848};
RA   Zhang Y.-J.;
RT   "Pseudooceanicola sediminis CY03 in the family Rhodobacteracea.";
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:RII37579.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QWJJ01000016; RII37579.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399IZ79; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000265848; 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..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   872 AA;  95741 MW;  B53440A768EFE61A CRC64;
     MDLTKFTERS RGFIQAAQTI AIRENHQRLL PEHILKALMD DDEGLASNLI GKAGGDVGAV
     TQALAVALKK VPVIGGDSGQ IYMDNQTVKV IAEAEKVAKQ AKDTFVPVER LLTALALVKG
     GARDTLEAGG VSAQKLNAAI NDIRKGRTAD TASAEDTFEA LEKYALDLTA RAEEGKIDPI
     IGRDDEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIINGDVPE SLRNKRLLAL
     DMGSLIAGAK YRGEFEERLK AILKEIESAA GEVILFIDEM HTLVGAGKAD GAMDAANLIK
     PALARGELHC IGATTLDEYR KYVEKDAALA RRFQPVMVSE PTVEDTISIL RGIKEKYELH
     HGVRISDSAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDQLDRNIL
     QMQIEIEALR NEDDAASKDR LETLERDLAD VQERSDSMTA KWQAERDKLA GARELKEQLD
     RARADLEIAK RNGDLARAGE LSYGIIPQLE KQLGEAEEQE AEGVMVEEAV RPEQIAQVVE
     RWTGIPTAKM LEGDREKLLR MEDGLHKRVI GQNSAVRALS NAVRRARAGL NDENRPLGSF
     LFLGPTGVGK TELTKAVAEY LFDDDNAMVR IDMSEFMEKH SVARLIGAPP GYVGYDEGGV
     LTEAVRRRPY QVVLFDEVEK AHPDVFNVLL QVLDDGVLTD GQGHKVDFKQ TLIILTSNLG
     AQALSRLPEG ADAGEAKRDV LEAVRAHFRP EFLNRLDEII VFDRLARKDM NGIVDIQMSR
     LLKRLAARKI TLQLDDGARQ WLADEGYDPV FGARPLKRVI QRVLQDPLAE ALLAGEVRDG
     DTVPVTAGAE GLLIGNRVGA SQRGKPDEAT VH
//
DBGET integrated database retrieval system