ID A0A022L1V6_9MICO Unreviewed; 886 AA.
AC A0A022L1V6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=D641_0105990 {ECO:0000313|EMBL:EYT49906.1};
OS Brachybacterium muris UCD-AY4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT49906.1, ECO:0000313|Proteomes:UP000019754};
RN [1] {ECO:0000313|EMBL:EYT49906.1, ECO:0000313|Proteomes:UP000019754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT49906.1,
RC ECO:0000313|Proteomes:UP000019754};
RX PubMed=23516213;
RA Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT "Draft genome sequence of an Actinobacterium, Brachybacterium muris strain
RT UCD-AY4.";
RL Genome Announc. 1:E0008613-E0008613(2013).
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:EYT49906.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AORC01000006; EYT49906.1; -; Genomic_DNA.
DR RefSeq; WP_017822902.1; NZ_AORC01000006.1.
DR AlphaFoldDB; A0A022L1V6; -.
DR STRING; 1249481.D641_0105990; -.
DR HOGENOM; CLU_005070_4_2_11; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000019754; 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};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000019754};
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"
SQ SEQUENCE 886 AA; 96695 MW; CCDC22FAF75B1863 CRC64;
MDFRFTTRSQ DAVTAAAEKA AELGNPQISA MHLLWALAEQ GDTIAHAALE EAGASPQEIA
QRAAEAVEAL PRVSGSGAAN PTFVGSGFDA LEAARKEADF QHKTYLSTEH LLIGIALGKD
DAARLLTSRG ARPGSLRDAV VRLHGGEQNM NQMDSQNPEN TFQSLEKFGV DLTEMAREGR
LDPVIGRDTE IRRVVQVLSR RTKNNPVLIG EPGVGKTAVV EGLAQRIVAG DVPDSLRGKK
LISLDLSSMV AGSKYRGEFE ERMKAVLDEI RTSNGQIITF IDELHTVVGA GGTGDGAMDA
GNMLKPMLAR GELRMVGATT LDEYRENIEK DPALERRFQQ VFVGEPSVES TITILRGLKD
KYEAHHKVSI TDAALVAAAT LSDRYIPGRQ LPDKAIDLVD EAASRQRMEL DSSPEELDIL
RRQVDRLKME EMALTGSEDP GSIAQLESVH SQLADRTERM TALSARWERE KAGLNLVGDL
KAQLEQLRMQ ADRAQREGDL TAASKILYGD IPALKEQLVQ AEEAEASGEG DGERPLVSDH
VGADDIAEVV GAWTGIPAGR LLQSETQKLL EMEDIIGRRL IGQKRAVTEV SDAVRRARAG
ISDPNRPTGS FLFLGPTGVG KTELAKALAE FLFDDERAMV RIDMSEYGEK HTVSRLVGAP
PGYVGYDEGG QLTEAVRRRP YSVVLLDEIE KAHPDVFDVL LQVLDDGRLT DGQGRTVDFR
STILILTSNL GAHVLQDSLL SQEEKNDKVM SVVRASFKPE FLNRLDDVVI FDPLNREELA
RIVTLQIKDV ASRLADRRIA LDVDQAATDW LAEKGFDPMY GARPLKRLVQ KEIGDALARL
ILKGEVHDGE HVEVTARQDG SGLDLVVAPE DGVVEAEPVE DEDQQG
//
