ID A0A0E3ZDM0_9BACT Unreviewed; 872 AA.
AC A0A0E3ZDM0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=PKOR_03520 {ECO:0000313|EMBL:AKD02365.1};
OS Pontibacter korlensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD02365.1, ECO:0000313|Proteomes:UP000033109};
RN [1] {ECO:0000313|EMBL:AKD02365.1, ECO:0000313|Proteomes:UP000033109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X14-1T {ECO:0000313|EMBL:AKD02365.1,
RC ECO:0000313|Proteomes:UP000033109};
RX PubMed=26057562; DOI=10.1038/srep10929;
RA Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT "Unraveling adaptation of Pontibacter korlensis to radiation and
RT infertility in desert through complete genome and comparative
RT transcriptomic analysis.";
RL Sci. Rep. 5:10929-10929(2015).
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; CP009621; AKD02365.1; -; Genomic_DNA.
DR RefSeq; WP_046309154.1; NZ_CP009621.1.
DR AlphaFoldDB; A0A0E3ZDM0; -.
DR STRING; 400092.PKOR_03520; -.
DR KEGG; pko:PKOR_03520; -.
DR PATRIC; fig|400092.3.peg.796; -.
DR HOGENOM; CLU_005070_4_2_10; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000033109; 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: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 78, MITOCHONDRIAL; 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:AKD02365.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AKD02365.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033109};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 397..529
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 97520 MW; 51660BBE0DE31A62 CRC64;
MNFNNYTIKA QEAIQKATEI AGGNQQQAID TGHILKAILE TDENVTNFLL QKLNINGNIL
HSKLDETVAA YPKVSGGSPY LANDAAAALQ KATSYLKEFG DEYVAIEHML LGLLAGRDKV
AGLMKDVGFN EKDLKKAIKE LRGGAKVTDQ NAEAKYNSLK RYARNLNELA RSGKIDPVIG
RDEEIRRVLQ ILSRRTKNNP VLLGEPGVGK TAIVEGLAQR MVSGDVPENL KNKTLMSLDM
GLLVAGAKYK GEFEERLKAV IKEVTDAEGE IILFIDEIHT LIGAGAGGDS AMDAANLLKP
ALARGELHAI GATTLKEYQK YIEKDKALER RFQAVMVDEP SVPDAISILR GIKDKYELHH
GVRIKDDAII SAVELSNRYI SDRFLPDKAI DLMDEAAAKL RIEIDSLPVE LDELQRRVMQ
LEIEREAIRR ENDKDKEAAL SKEIADLSGK RDDLKAKWQN EKQIIEGIQK AKENIENFKL
EAEQAERAGD YGRVAELRYG KIQEAEAHLK QLQEQVREMQ GENPMLKEEV NSEDIAEVVA
KWTGIPVSKM LQSDREKLLH LEQELGKRVA GQEEAIEAIS DAVRRSRAGM QDPKRPIGSF
IFLGTTGVGK TELAKALADY LFNDDNAMVR IDMSEYQERH AVSRLIGAPP GYVGYDEGGQ
LTEAIRRKPY SVVLLDEIEK AHPDVFNILL QVLDDGRLTD SKGRVVNFKN TIIIMTSNIG
SHIIQANFEK MTPLNHDEVI EQTKEEVFDL LKKSVRPEFL NRIDELVMFR PLSRGDIRKI
VSIQFRHIQH RLEEAGIQLI ATDEVLDYLG EQGFDPQFGA RPLKRVIQRQ VLNELSKEIL
SGKINKDSVV EAVLENGEIL FNNVDVEIPT GK
//
