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Database: UniProt
Entry: A0A4P9K8K9_9GAMM
LinkDB: A0A4P9K8K9_9GAMM
Original site: A0A4P9K8K9_9GAMM 
ID   A0A4P9K8K9_9GAMM        Unreviewed;       856 AA.
AC   A0A4P9K8K9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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:QCU90746.1};
GN   ORFNames=FE785_08955 {ECO:0000313|EMBL:QCU90746.1};
OS   Thiomicrorhabdus sediminis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrorhabdus.
OX   NCBI_TaxID=2580412 {ECO:0000313|EMBL:QCU90746.1, ECO:0000313|Proteomes:UP000304864};
RN   [1] {ECO:0000313|EMBL:QCU90746.1, ECO:0000313|Proteomes:UP000304864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:QCU90746.1,
RC   ECO:0000313|Proteomes:UP000304864};
RA   Liu X.;
RT   "Thiomicrorhabdus sediminis sp. nov, a novel sulfur-oxidizing bacterium
RT   isolated from coastal sediment.";
RL   Submitted (MAY-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. {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; CP040602; QCU90746.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4P9K8K9; -.
DR   KEGG; thig:FE785_08955; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000304864; 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:UP000304864};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          2..141
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          407..521
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   856 AA;  95319 MW;  00B2B1FD9F92278E CRC64;
     MMDKFTTQFQ NALAQAQSIA VGQDNQFIEP LHILSALIDE SSHLLQLAQV NTALLKQSVQ
     EKLNSLPKVS GSAGNVQLSQ KSAQVLNLMD KQAQQNADAF IASELFYLAL LETNDTAATL
     LKQAGADKNK IEQAIQQVRG GESVQDQNAE QNRQALEKYT IDLTERAESG KLDPVIGRDD
     EIRRAVQVLQ RRTKNNPVLI GEPGVGKTAI VEGLAQRIVN GEVPEGLKNK RLLSLDLAGL
     LAGAKYRGEF EERLKGLLKD LEKQAGQVIL FIDEIHTMVG AGKTEGSMDA GNMLKPALAR
     GELHCIGATT LNEYRENIEK DAALERRFQK VIVDEPSEED TIAILRGLKE RYEVHHGVDI
     TDPAIVAAAS LSQRYITDRQ LPDKAIDLID EAASRIRMEI DSKPEVMDRL DRRLIQLKME
     QVALKKEKDE ASKKRLASLQ EQIAEMEKEY SDLEEIWKKD KAALQGAQQF KEKLEQARID
     LESARREGNL AKMSEIQYGK IPELETKIRE AEMAESAASE ESEQHLLRNK VTEEEIAEVV
     ARWTGIPVAK MMQGEREKLL EMEQVLEEQV VGQREAVKAV SDAIRRSRAG LSDPNRPNGS
     FLFLGPTGVG KTELTKALAD FLFDTTDAIV RIDMSEFMEK HSVARLVGAP PGYVGYEQGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFK NTVIVMTSNL
     GSQVIQEKAG KASYAEMKSD VMEVVGNYFR PEFINRIDDI VVFHPLAQEQ IRAIANIQLD
     SLRQRLAAND MQLEISDAAL DMIGEVGFDP VFGARPLKRV IQQQVENPLA QKILQGDFSP
     GGTVHIDYQN EKLSFD
//
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