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
//