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Database: UniProt
Entry: A0A222FQA8_9GAMM
LinkDB: A0A222FQA8_9GAMM
Original site: A0A222FQA8_9GAMM 
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
//
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