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Database: UniProt
Entry: A0A372IFX9_9RHOB
LinkDB: A0A372IFX9_9RHOB
Original site: A0A372IFX9_9RHOB 
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
//
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