ID A0A1R4H547_9GAMM Unreviewed; 858 AA.
AC A0A1R4H547;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:SJM91306.1};
GN ORFNames=CRENPOLYSF1_190013 {ECO:0000313|EMBL:SJM91306.1};
OS Crenothrix polyspora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Crenotrichaceae; Crenothrix.
OX NCBI_TaxID=360316 {ECO:0000313|EMBL:SJM91306.1, ECO:0000313|Proteomes:UP000195667};
RN [1] {ECO:0000313|EMBL:SJM91306.1, ECO:0000313|Proteomes:UP000195667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSM_CP1 {ECO:0000313|EMBL:SJM91306.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUKI01000092; SJM91306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4H547; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000195667; 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:UP000195667};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 95571 MW; B844A299B9676978 CRC64;
MRMDKLTHKF QTALSDAQSL ALGKDHQFIE PVHLLIALLD QEGGSIKPLL AQLGGNVQIL
RAELTKEIAR IATVSGSGGN VQISNELSRL LNMTDKLAQK RNDAFISSEL FLLAIFEEKG
FLQDLFKKIG LTKQDIEKAI DAMRGGEAVG DANAEDQRQA LKKYTINLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SMKHKQVLSL
DMAALIAGAK FRGEFEERLK AVLNDLAKQE GQVILFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR KYVEKDAALE RRFQKVMVDQ PSVEDTIAIL RGLKEKYEVH
HGVDITDPAI VAAATLSYRY ISDRQLPDKA IDLIDEAASR IRMEMDSKPE EMDKLYRRLI
QLKIEQVALK KEADAASKKR LGILEQDIGE LEKEYSDLEE IWKAEKASLQ GSAAIKEKLE
HARGELEAAS RTNDLAKMSE LQYGIIPALE KQLDTVVSSE GQKMTLLRNK VTEDEIAEVV
SKWTGIPVSK MMEGERDKLL RMEEQLNKRV IGQEEALKAV SNAIRRSRAG LSDPNRPNGS
FLFLGPTGVG KTELCKALAE FLFDTPDAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTELVRRKP YSVILLDEIE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
GSTRIQELAG EVNYHAMKEA VMEIVGHQFR PEFINRIDEA VVFHPLDQQQ IRAISCIQIE
FLRKRLLDRD IGFEIDDNAL DILGEAGFDP VYGARPMKRA IQQQLENPLA QSILAGEFVA
GDTIVVNVLN DSLHFSKK
//