ID A0A1B8U1M4_9FLAO Unreviewed; 868 AA.
AC A0A1B8U1M4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=LPB301_08125 {ECO:0000313|EMBL:OBY65773.1};
OS Polaribacter reichenbachii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=996801 {ECO:0000313|EMBL:OBY65773.1, ECO:0000313|Proteomes:UP000092612};
RN [1] {ECO:0000313|Proteomes:UP000092612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 23969 {ECO:0000313|Proteomes:UP000092612};
RA Shin S.-K., Yi H.;
RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL Submitted (FEB-2016) 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:OBY65773.1}.
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DR EMBL; LSFL01000029; OBY65773.1; -; Genomic_DNA.
DR RefSeq; WP_068359994.1; NZ_VRMM01000008.1.
DR AlphaFoldDB; A0A1B8U1M4; -.
DR STRING; 996801.BW723_13655; -.
DR KEGG; prn:BW723_13655; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000092612; 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 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:UP000092612};
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..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 97787 MW; 9BAB029B3CDB3AF4 CRC64;
MNFNNYTTKS QETIQMAQQI AQSFGHNQIE NEHIFKALTQ VDENVLPFLL KKLNINIDVV
TQILDKQLES LPKVSGAELM LSREAGKSLN EASIIAKNMK DDYVSIEHLI LAIFKSKSNI
AQVLKDQGVT EKHLKAAIDE LRKGERVTSQ SQEETYNSLN KFAKNLNQLA QDGKLDPVIG
RDEEIRRLLQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IVDGDVPENL KDKLIFSLDM
GALIAGAKYK GEFEERLKAV IKEVTTSDGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVIVDEPD TESAISILRG IKEKYETHHK
VRIKDEAIIG AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE KDEVKLKSLR SDLANLKEER NEINAKWKSE KEVVDNIQNA KMDIESFKIE
AEKAEREGNY GLVAELRYGK IKKAQEDLEV LQKNLQENQS EKSLIKEEVT LDDIAEVVAK
WTGIPVTKMI QSEREKLLFL ENQLHKRVVG QEEAIVAVSD AVRRSRAGLQ NPNKPIGSFL
FLGTTGVGKT ELAKALAEYL FDDENAMTRI DMSEYQERHS VSRLVGAPPG YVGYDEGGQL
TEAVRRRPYS VVLLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRVADFKNT IIIMTSNMGS
HIIQEKFADP KADLEAVTEL AKIEVLGLLK QSVRPEFLNR IDDVIMFTPL NQSDIFEIVK
LQIEHLKKMI GKQEITLDAT DEAITYLAKK GYQPEFGARP VKRVIQKEVL NQLSKEILSG
KVTTDSIILL DAFDDELVFR NQSDLVVN
//