ID A0A0G1P4S9_9BACT Unreviewed; 895 AA.
AC A0A0G1P4S9;
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=UW93_C0007G0034 {ECO:0000313|EMBL:KKT91419.1};
OS Parcubacteria group bacterium GW2011_GWC1_45_13.
OC Bacteria.
OX NCBI_TaxID=1618914 {ECO:0000313|EMBL:KKT91419.1, ECO:0000313|Proteomes:UP000034639};
RN [1] {ECO:0000313|EMBL:KKT91419.1, ECO:0000313|Proteomes:UP000034639}
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:KKT91419.1}.
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DR EMBL; LCKG01000007; KKT91419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1P4S9; -.
DR PATRIC; fig|1618914.3.peg.562; -.
DR Proteomes; UP000034639; 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 4..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 415..496
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 895 AA; 100952 MW; A7D3AAC1C02C6D3E CRC64;
MPPYGQFTIK AQEALKRAHE LAIERGGSQI DAMHLLAALL LQEDGVIPSL LDKLETDQAN
LVDLVMGELD NTLRTNILSP SHQIYLTPEL ARVLEEAHKS ASFLKDEFIS TEHLFLGILE
APSRAREILG RFSLNREMIL RALADIRGSQ RVTDVEPENK YRALEKYARN LTRLAREDKL
DPVIGRDEEI RRVMQVLSRR TKNNPVLIGE AGVGKTAIVE GLASRIASGD VPETLKDKEL
ISLDLGALVA GTKYRGEFEE RLKAVMKELE RAAGKVLLFI DEVHTLVGAG AAEGAMDASN
MLKPALARGE LHAIGATTIK EYQKYIEKDA ALARRFQPVL VDEPSLEDTV SILRGIKNKY
ELHHGIKITD AAITTAVNLS ARYITDRFLP DKAIDLIDEA ASSLRLQMDS MPDELEHTRR
EVMKLEIEKE ALKKEESNPE AKQKIRKIQK QIDELKEETA GLEMRWKHEK ETIDAIRQLK
KDLEIFRQES DAAERRGDLA KVAEIRYGRI PESEKMLYAE EGKLRKIQGT RRILREEITE
EDIADIVSRW TGIPVRRMLE SEAKKLLRME EELKKRVIGQ AEAIEKISQA IRRSRAGIAD
EKRPIGSFMF LGPTGVGKTE LALTLSEFLF NDEKALVRVD MSEYMERHAV SKFIGSPPGY
VGYEEAGNLT ETIRHRPYAV LLFDEIEKAH PEVFNIMLQI LDNGTLTDAK GRHVNFKNTV
IIMTSNIGGE FIREMGSLGF VGGAVDRVKK EDDLKTKILR SLEQHYRPEF LNRLDEVIIF
NSLQPEELKQ IAKIQIARLT ERISARGISV SVNKSAEDAL AKEGYDPNYG ARPLRRLIQN
KILNPLAEKI ISKQIKEGDT ALVDFRSGAF VIEVKKLLSA LPKKEKDKKV KITTT
//
