ID A0A1N6GGW6_9GAMM Unreviewed; 857 AA.
AC A0A1N6GGW6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05443662_1334 {ECO:0000313|EMBL:SIO06701.1};
OS Sulfurivirga caldicuralii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Sulfurivirga.
OX NCBI_TaxID=364032 {ECO:0000313|EMBL:SIO06701.1, ECO:0000313|Proteomes:UP000198461};
RN [1] {ECO:0000313|EMBL:SIO06701.1, ECO:0000313|Proteomes:UP000198461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17737 {ECO:0000313|EMBL:SIO06701.1,
RC ECO:0000313|Proteomes:UP000198461};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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. {ECO:0000256|RuleBase:RU362034}.
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|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; FSRE01000003; SIO06701.1; -; Genomic_DNA.
DR RefSeq; WP_074201605.1; NZ_FSRE01000003.1.
DR AlphaFoldDB; A0A1N6GGW6; -.
DR STRING; 364032.SAMN05443662_1334; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198461; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:SIO06701.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SIO06701.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198461};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 2..142
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 401..522
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 857 AA; 95658 MW; 6AD81F2ADB405C63 CRC64;
MMDRMTNALQ QALQDAQSKA VENSNQFIEP LHILDALIEP QGNLLRLAGV DVNTLRQKVA
EKLKTLPQVS GAAAGDVKIS NKTAQVLNLM DKQSKEMGDS YIASELFFLA LLEVADIAAD
LLKEAGASKE KLLEAIQKIR GGETVQDPNA EDTRQALEKY TIDLTARAAE GKLDPVIGRD
DEIRRTIQVL QRRTKNNPVL IGEPGVGKTA IVEGLAQRIV NKEVPEGLRD KRVLSLDLGA
LLAGAKYRGD FEERLKALIK DIEKSEGQII LFIDEIHTMV GAGKADGAMD AGNMLKPALA
RGELHVIGAT TLDEYRQYIE KDAALERRFQ KVLVDEPSVE DTIAILRGLK ERYEVHHGVE
ITDSAIVAAA TLSHRYITDR KLPDKAIDLI DEAASRIRME IDSKPEELDK LERRLIQLKI
EREALKKEKD EAAKKRLAEL EEKIAELEKQ YAELEEIWKR DKALLQGVKE LKAQLDKARI
ELEQALREGN MNRAAELQYG VIPELERKIK EAEEAEANAD EQPHLLRNKV TEEEIAEVVS
RWTGIPVSKM LEGEREKLLH LEDELRKRVV GQDEAVHAVA AAIRRARAGL ADPNRPNGSF
LFLGPTGVGK TELTKALAEV LFDTEEAIVR LDMSEFMEKH AVARLIGAPP GYVGYEEGGY
LTEKVRRKPY SVILFDEVEK AHPDVFNILL QVLDDGRLTD SHGRTVDFRN TVIIMTSNLG
SHLIQEMAGV KDYEAMKAAV MEVVGQHFRP EFINRIDETV VFHPLGKAQI RAITNIQIRR
VARRLEEQDI KLQVSEAALD LLGEAGFDPV YGARPLKRAI QHLLENPLAE RLLKGEFAPG
DTIIVDVENG DLAFRKG
//