ID A0A0G0MHJ9_9BACT Unreviewed; 871 AA.
AC A0A0G0MHJ9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=UT31_C0017G0002 {ECO:0000313|EMBL:KKR03534.1};
OS Parcubacteria group bacterium GW2011_GWF2_39_13b.
OC Bacteria.
OX NCBI_TaxID=1618962 {ECO:0000313|EMBL:KKR03534.1, ECO:0000313|Proteomes:UP000034319};
RN [1] {ECO:0000313|EMBL:KKR03534.1, ECO:0000313|Proteomes:UP000034319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:RU362034}.
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:KKR03534.1}.
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DR EMBL; LBWH01000017; KKR03534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MHJ9; -.
DR PATRIC; fig|1618962.3.peg.262; -.
DR Proteomes; UP000034319; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362034};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU362034};
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:RU362034};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 50..106
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 407..535
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 97944 MW; 1EB2620DB6841EDD CRC64;
MQIDRFTIKA QEALRDAHII ATQKNHQQIN TVHLLAALTR QKNTVVVPLL ERLDVNAGFL
EAEIEKEMSR LAQISGDTQV GQIFITQELN KVLNIASQSA KNLQDEYISC EHLLLAIIEA
SPKLKEILKS FGVTSQKILE VLKDVRGAQH VTDIEPESKY QVLEKYARNL TDLARQEKLD
PVIGRDEEIR RVMQVLSRRT KNNPVLIGEA GVGKTAIAEG LAQRIVAGDV PESIKEKELI
ALDLGSLVAG TKFRGEFEDR IKAVLKEIDR SAGKYILFID ELHTLVGAGA AEGSIDASNL
LKPALARGEL RAIGATTLKE YQKYIERDPA LERRFQPVTI IEPTIEDTVA ILRGIKEKYE
VHHGVRITDP ALVAAANLSS RYITDRFLPD KAVDLMDEAA SALRMEIDSM PTELDQAKRR
MMKLEIERQA LKKEKTSEGR AKLKKIEKDL AELKESTGSL EMRWKTEKNI ISKIRELKAK
IEKLKQEADI AERSGELQKV AEIRYGQILE IEKEAKAQQK KLAEIQKTNP ILKEEIGEAD
VARVVARWTG IPVERMLESE AEKLTRMESE LHKRIVDQED AIKAVAAAVR RARAGIAEEN
KPIGSFMFMG PTGVGKTELS KALAEFMFND EKAIIQIDMS EYMEKHAVSR MVGSPPGYVG
YEEGGQLTEA VRRRPYSVIL LDEIEKAHPE AFNLLLQVLD NGRLTDGKGR VVNFKNTVII
MTSNIGNEII KRFVLGFGEG GKEEEKISKD EVKERVMEAL RRQFKPEFIN RIDEIIVFDS
LSKENLVKIV DLQLEKLSKR LIEKKIKIKV SAKAKKLLVE KGYDPNYGAR PLKRVIQQLI
LDEIAKAMIA GKIKEGAKVE IDAEDNKIII K
//
