ID A0A222FQA8_9GAMM Unreviewed; 865 AA.
AC A0A222FQA8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:ASP40423.1};
GN ORFNames=CHH28_17830 {ECO:0000313|EMBL:ASP40423.1};
OS Bacterioplanes sanyensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Bacterioplanes.
OX NCBI_TaxID=1249553 {ECO:0000313|EMBL:ASP40423.1, ECO:0000313|Proteomes:UP000202440};
RN [1] {ECO:0000313|EMBL:ASP40423.1, ECO:0000313|Proteomes:UP000202440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NV9 {ECO:0000313|EMBL:ASP40423.1,
RC ECO:0000313|Proteomes:UP000202440};
RA Rehman Z.U.;
RT "Annotated genome sequence of Bacterioplanes sanyensis isolated from Red
RT Sea.";
RL Submitted (JUL-2017) 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; CP022530; ASP40423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222FQA8; -.
DR KEGG; bsan:CHH28_17830; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000202440; 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:UP000202440};
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 865 AA; 95505 MW; E5178A3C82EEF5E4 CRC64;
MRMDRLTTSL QNALAESQSL ALGHDHNHID TIHVLLALLE QPSSSVKDVL RRAGAQVPAL
ERALRQALGD LPRVSSPDGN IQLAPELGRI LNLADKEAQK LGDQYVSSEV FLLVALQDKG
AAGKALNQAG VSGAQLSAAI KDMRGGENVS DAHAEDNRQS LDKYCIDLTE RAEAGKLDPV
IGRDDEIRRT VQVLQRRTKN NPVLIGPPGV GKTAVVEGLA QRIVDGEVPE NLKNKRILAL
DMGALVAGAK YRGEFEERLK AVLKDVAKEE GRIVLFIDEM HTMVGAGKSD GAMDAGNMLK
PALARGELHC VGATTLDEYR EFVEKDAALE RRFQKVLVDE PSVEDTIAIL RGLKERYEVH
HGVQITDSAI IAASKLSQRY ISDRRLPDKA IDLVDEAASV IRMEIDSKPQ DMDKLERRLI
QLKIEREALR KEKDEAAKKR LSDLNEEINK AGTAYVDLEE VWKKEKALLE GASQAKEQLE
QARIELEAAR RAGDLQKMSE LQYGRIPELE KQLASANEAE TSGTQEFTLL RNKVTEDEIA
EVVSKWTGVP VNKMLEGERE KLLRMEDVLH DSVVGQQQAI AAVSNAVRRS RAGLSDPNRP
NGSFLFLGPT GVGKTELCKA LATFLFDSKD AMVRIDMSEY MEKHSVARLI GAPPGYVGYE
EGGYLTEAVR RKPYSVILLD EVEKAHPDVF NILLQVLDDG QLTDGQGRRV DFKNTVLVMT
SNLGSDVIQT LASNDSVTTS YEDMREAVMG IVSSHFRPEF INRIDEAVVF HPLEKTQIRG
IAEIQLQLLH QRLAERELSL ELSEAAINQL VDVGYDPVFG ARPLKRAIQR SIENPLAQAI
LAGEFVPGSK IVADVQDHEF VFKAS
//