ID A0A2U2J7Q3_9FLAO Unreviewed; 868 AA.
AC A0A2U2J7Q3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PWG04370.1};
GN ORFNames=DIS07_13270 {ECO:0000313|EMBL:PWG04370.1};
OS Polaribacter aquimarinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2100726 {ECO:0000313|EMBL:PWG04370.1, ECO:0000313|Proteomes:UP000245670};
RN [1] {ECO:0000313|EMBL:PWG04370.1, ECO:0000313|Proteomes:UP000245670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY113 {ECO:0000313|EMBL:PWG04370.1,
RC ECO:0000313|Proteomes:UP000245670};
RA Lu D.;
RT "Polaribacter aquimarinus sp. nov., isolated from sediment in a sediment of
RT sea.";
RL Submitted (MAY-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWG04370.1}.
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DR EMBL; QFFG01000006; PWG04370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2J7Q3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000245670; Unassembled WGS sequence.
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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000245670};
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 410..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 97732 MW; 721BB5FFD45F7DE1 CRC64;
MNFNNYTTKS QETIQLAQQI AQGFGHNQIE NEHIFKALTQ VDENVLPFLL KKLSINNNVI
EQILDKQLES LPKVSGAELM LSREAGKSLN EAAIIAKNMK DDYVSIEHLI LAIFKSKSNI
AQVLKDQGVT EKHLKAAIEE LRKGERVTSQ SQEETYNSLN KYAKNLNDLA KNGKLDPVIG
RDEEIRRLLQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IVDGDVPENL KDKLIFSLDM
GALIAGAKYK GEFEERLKAV IKEVTTSDGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVLVDEPD TESAISILRG IKEKYETHHK
VRIKDEAIIG AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE KDEAKLKSLR SDLANLKEER NTINAKWKSE KEVVDNIQNA KLDIENFKIE
AEKAEREGDY GKVAEIRYGK IKQAQEKLEE YQQILAENQN GNSLIKEEVT YEDIAEVIAK
WTGIPVTKMI QSEREKLLHL EKQLHKRVVG QEEAIVAISD AVRRSKAGLQ NPNKPIGSFL
FLGTTGVGKT ELAKALAEYL FDDENAMTRI DMSEYQERHS VSRLVGAPPG YVGYDEGGQL
TEAVRRRPYS VVLLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRVADFKNT IIIMTSNMGS
HIIQEKFADP KADLDAVTEL AKIEVLGLLK QSVRPEFLNR IDDVIMFTPL TQSNIFEIVS
LQLDSLKKMI GKQEITLDAT DEAIKYLAKR GYQPEFGARP VKRVIQKEVL NQLSKEILSG
KITTDSIILL DAFDDKLVFR NQSDLVEN
//
