ID U1R7S2_9BIFI Unreviewed; 873 AA.
AC U1R7S2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=HMPREF9244_01672 {ECO:0000313|EMBL:ERH29609.1};
OS Alloscardovia omnicolens F0580.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Alloscardovia.
OX NCBI_TaxID=1321816 {ECO:0000313|EMBL:ERH29609.1, ECO:0000313|Proteomes:UP000016519};
RN [1] {ECO:0000313|EMBL:ERH29609.1, ECO:0000313|Proteomes:UP000016519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0580 {ECO:0000313|EMBL:ERH29609.1,
RC ECO:0000313|Proteomes:UP000016519};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-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|ARBA:ARBA00004496,
CC 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:ERH29609.1}.
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DR EMBL; AWSI01000043; ERH29609.1; -; Genomic_DNA.
DR RefSeq; WP_021618778.1; NZ_KE952646.1.
DR AlphaFoldDB; U1R7S2; -.
DR STRING; 419015.HMPREF3214_00266; -.
DR GeneID; 56317094; -.
DR PATRIC; fig|1321816.3.peg.1474; -.
DR HOGENOM; CLU_005070_4_2_11; -.
DR Proteomes; UP000016519; 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 Reference proteome {ECO:0000313|Proteomes:UP000016519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 873 AA; 95496 MW; 53E96C8ADFE4CEA3 CRC64;
MEQKFTTMAQ EAISSAVQSA SAAGNPQVET LHLVDALLNQ EQGVVRGLLE ATGADVQSIG
AAIRNALVAL PQVSGNTTTQ ASAARSVEVA LVDAQKIMSK MGDEYISTEH LLIAVAQGQS
QAADILKKFG ATAQALTQAV PSVRGGAKVT SPDAEGSYKA LEKYSTDLTA RAREGKLDPV
IGRDKEIRRV IQILSRRTKN NPVLIGEPGV GKTAVVEGLA QRVVAGDVPT TLQNKRVITL
DMSSMVAGSK YRGEFEERLK AVLEEIQRAE GNIITFIDEI HTIVGAGATE GSMDAGNMLK
PMLARGELRL IGATTLDEYR ENIEKDPALE RRFQQVFVGE PSVEDTVAIL RGLKERYEAH
HKVTIGDDAL VAAATLSNRY ISGRQLPDKA IDLVDEAAAH LRMELDSSPE EIDELSRRVT
RLEMEEMQLK KSEDIASQER LEKLQSELAD TREQLAGLNA RWESEKSGHN KVGDLRAQLD
ALRVEADKAT REGDLEKASR ILYGDIPSIQ KELAAAEKNA DDSKAEQSET EPMVPDHVDA
DSIAQIVSDW TGIPVGRLMQ GENEKLLHME DELGKRVIGQ KEAVRAVSDA VRRSRAGISD
PNRPTASFMF LGPTGVGKTE LAKALADFLF DDERAVVRID MSEYMEKSSV SRLIGAAPGY
IGYEEGGQLT EAVRRRPYSV VLFDEVEKAH PEVFDILLQV LDDGRLTDGQ GRTVDFKNTI
LIMTSNLGSQ FLVSSELEGE ARKQAVMNAV HAHFKPEFIN RLDDLIVFDP LTRDELAHIV
DIQVKAVADR LTERRITLNV TKSAREWLAD RGYDPAFGAR PLRRLVQSEV GDQLARMLLS
GAVHDGDTVL VDQTGGEHLE LSSWATEDVQ LND
//
