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Database: UniProt
Entry: A0A5B9ESW4_9RHOB
LinkDB: A0A5B9ESW4_9RHOB
Original site: A0A5B9ESW4_9RHOB 
ID   A0A5B9ESW4_9RHOB        Unreviewed;       871 AA.
AC   A0A5B9ESW4;
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:QEE36861.1};
GN   ORFNames=FTO60_14785 {ECO:0000313|EMBL:QEE36861.1};
OS   Octadecabacter sp. SW4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=2602067 {ECO:0000313|EMBL:QEE36861.1, ECO:0000313|Proteomes:UP000323131};
RN   [1] {ECO:0000313|EMBL:QEE36861.1, ECO:0000313|Proteomes:UP000323131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SW4 {ECO:0000313|EMBL:QEE36861.1,
RC   ECO:0000313|Proteomes:UP000323131};
RA   Baek K.;
RT   "Octadecabacter sp. SW4 isolated from Artic Sea Water.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP042819; QEE36861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5B9ESW4; -.
DR   KEGG; oct:FTO60_14785; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000323131; Chromosome.
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:UP000323131};
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..439
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  95304 MW;  02D1179B245E2E30 CRC64;
     MNLEKFTERS RGFVQAAQTI AMRESHQRLS PEHLLKALLD DEQGLAANLI DRSGGNAKRV
     LEQVDLAVGK LTKVTGDAGQ VYLDSATGKV LDEAEKIATK AGDSFVPVER ILMALAMVKS
     KAKDALDAGG VNAQSLNATI NDIRKGRTAD SASAEDSYDA LKKYARDLTE AAEQGKIDPI
     IGRDEEIRRS MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLRNKKLMAL
     DMGALIAGAK YRGEFEERLK AVLNEVTDAA GEIILFIDEM HTLVGAGKSD GAMDAANLIK
     PALARGELHC IGATTLDEYR KYVEKDAALA RRFQPLVVEE PTVEDTVSIL RGIKEKYELH
     HGVRISDSAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDRQIL
     QLQIEAEALK KEDDAASKDR LETLEKELGD LVDRSDAMTV KWQAERDKLE GARGLKEQLD
     RARAELDIAK REGNLQKAGE LSYGVIPKLE KQIGEAEGGE TDLMVEEAVR PEQIASVVER
     WTGVPVSKML EGEREKLLRM EDGLHKRVIG QDSAVKAVAN AVRRARAGLN DEGRPLGSFL
     FLGPTGVGKT ELTKAVAEFL FDDDNAMVRI DMSEFMEKHA VSRLIGAPPG YVGYDEGGVL
     TEAVRRRPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRTVDFKQT LIVLTSNLGA
     QALSQLPDGG DMAEAKRDVM DAVRAHFRPE FLNRLDETII FDRLARADMN GIVDIQLGRL
     EKRLAGRKIM LDLDEGARKW LADEGYDPVF GARPLKRVIQ RALQDQLAEM ILAGDVLDGD
     TVPVSAGADG LIVGDRVAGS NRPKPDDAVV H
//
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