ID A0A0R2SAY7_9FLAO Unreviewed; 855 AA.
AC A0A0R2SAY7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ABR83_07755 {ECO:0000313|EMBL:KRO72041.1};
OS Cryomorphaceae bacterium BACL18 MAG-120924-bin36.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655591 {ECO:0000313|EMBL:KRO72041.1, ECO:0000313|Proteomes:UP000051105};
RN [1] {ECO:0000313|EMBL:KRO72041.1, ECO:0000313|Proteomes:UP000051105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL18 MAG-120924-bin36 {ECO:0000313|EMBL:KRO72041.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRO72041.1}.
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DR EMBL; LIBP01000075; KRO72041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2SAY7; -.
DR Proteomes; UP000051105; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..142
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 408..485
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 855 AA; 94681 MW; 08DD0D0E9689CF11 CRC64;
MDNLTVKTQS ALQAAQQRAT ELGHQAIDSA HLFVGAVEAD RAFIEDLLRR AGLVPETLVR
TAEALLAQHG RVDGGERYLS RPAQNALAQA ATAAKKFGDD YVSLEFLIMG IGTASDAMGQ
ALRDAGFREK EFSAVIAQLR QGKKAQSASA EGSYQALKKY AIDLNERAES GKLDPVIGRD
DEIRRVLQIL SRRTKNNPVL VGEPGVGKTA IAEGLAHRIV RGDVPENLQG KRIFSLDMGS
LIAGAKYKGE FEERLKSVIQ EVTAAEGDLI LFIDEIHTLV GAGGGEGAMD AANILKPALA
RGELRCVGAT TLNEFQKYFE KDKALERRFQ KVLVEEPDTE ASIAILRGIK EKYESHHKVR
IKDEAVVQAV LLSQRYISDR FLPDKAIDLM DEAASKLRLE INSKPEELDD LDRKIIQLEI
EREAIQREDD PKRLNLLKQE LAALNEKRTA LGAQWSAEKE AVERIQRAKE DVERLKLEAE
QAERNGYYAK VAEIRYGKLA AAEQSITDGL AALDELRTDR RAMVQEEVGA EDIAEVVSRW
TGIPVSKMLE SERSKLLRLE DELHQRVVGQ NEAIEAVSDA LRRARAGLGD PKRPIGSFLF
LGPTGVGKTE LARALAEFLF DDDQAMVRID MSEYQERHSV SRLVGAPPGY VGYEEGGQLT
EAVRRRPYAV VLLDEIEKAH PEVFNVLLQV LDDGRLTDGK GRTVNFTHSV VVMTSNLGSE
LLLDGEGPEA VQQLLRKTLR PEFLNRIDEI ITFHPLGEDH VRRIVQLQLK EVQKRLADQE
ITIEFTPEAV DALAAEGFDP AFGARPLKRT VQRRILNDLA KKLLSGEVQR DAVMLCDAVD
GAIFFTNTQL GLSQA
//
