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
//