ID U2TJH6_9ACTN Unreviewed; 868 AA.
AC U2TJH6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:ERL13209.1};
GN ORFNames=HMPREF1248_1184 {ECO:0000313|EMBL:ERL13209.1};
OS Coriobacteriaceae bacterium BV3Ac1.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae.
OX NCBI_TaxID=1111135 {ECO:0000313|EMBL:ERL13209.1, ECO:0000313|Proteomes:UP000016652};
RN [1] {ECO:0000313|EMBL:ERL13209.1, ECO:0000313|Proteomes:UP000016652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3AC1 {ECO:0000313|Proteomes:UP000016652};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-2013) 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: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:ERL13209.1}.
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DR EMBL; AWUP01000005; ERL13209.1; -; Genomic_DNA.
DR AlphaFoldDB; U2TJH6; -.
DR PATRIC; fig|1111135.3.peg.318; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000016652; 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 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000016652};
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..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 95588 MW; 1968E38D252BCA11 CRC64;
MRIDKWAVSA QEALQAAMGI AADADAGQME SIHLLKALLD SNEQNLRAIV ERIGVDPTQL
ESVVSDAIAR QPKVTGAGGQ MSIGNNLLKV LDAAEKLASQ MGDSYVTTEH LLIALCDDRD
AAGSVLKTAG VTAKRVRAAY DELRGDERVT SQDSKPQLKA LEQFGRNVTD LARQGKLDPV
IGRVEEIRRT IQVLSRRSKN NPVLIGEPGV GKTAIVEGLA QRIVTGDVPS TLKDKDLVEL
DMSALVAGAK YRGEFEDRLK SVLKEVQKSD GKVILFIDEL HTIVGAGATE GSMDAGNILK
PALARGELHA IGATTLDEYR KYIEKDQALA RRFQPVLVSE PTVEDTISIL RGIKERYEQH
HRVRITDAAL VAAADLSNRY ISERFLPDKA IDLVDEAASR LRMELDSMPA DIDAQERQLT
QMQIEEQALM KEEDAASKER LETLRREIAE AREKLDSVKA DWQNERVAID RVQDLKAQIE
STRSEMERVT REGDLARASE LRYSTIPQLQ AQYEEAEQAL ASKQESGGLL KEEVTTDEIA
EVVSNWTGVP VSKMMQGEMD KLKHLEDELH KSVVGQDEAV SAVAAAVRRS RAGLADPNRP
IGSFFFLGPT GVGKTELAKA LAKNLFDDER ALIRIDMSEY MEKFSVQRLI GAPPGYVGYD
EGGQLTEAVR RRPYSVILLD EMEKAHPDVF NVLLQVLDDG RLTDGQGRVV SFKNTIIIMT
SNVGSQFIAE ANATTDPKET QRQVNEALRA TFRPEFLNRI DDVVMFHALG LDDIEKIVDI
QLADVRERLA NERITLQLTP RAVGSLALDG LDPIYGARPL KRLIQRQVVD NVANLVIAGE
LHEGDTVQID VGEGDKLVAQ KLGDSAKS
//