ID L7LEN6_9ACTN Unreviewed; 852 AA.
AC L7LEN6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:GAC58493.1};
GN ORFNames=GOHSU_41_00310 {ECO:0000313|EMBL:GAC58493.1};
OS Gordonia hirsuta DSM 44140 = NBRC 16056.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1121927 {ECO:0000313|EMBL:GAC58493.1, ECO:0000313|Proteomes:UP000053405};
RN [1] {ECO:0000313|EMBL:GAC58493.1, ECO:0000313|Proteomes:UP000053405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16056 {ECO:0000313|EMBL:GAC58493.1,
RC ECO:0000313|Proteomes:UP000053405};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia hirsuta NBRC 16056.";
RL Submitted (DEC-2012) 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:GAC58493.1}.
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DR EMBL; BANT01000041; GAC58493.1; -; Genomic_DNA.
DR RefSeq; WP_005942737.1; NZ_BANT01000041.1.
DR AlphaFoldDB; L7LEN6; -.
DR STRING; 1121927.GOHSU_41_00310; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000053405; 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:UP000053405};
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 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 852 AA; 92684 MW; B17B7796238E7B4D CRC64;
MDSFTPTTKT QAALQAAVQD AAAAGNPDVR PAHILVALLE QSDGIATPLL KAVGVDPAHM
LAEAKALVSR APVVSSTSAQ PQLSRESIAA ISTAQNLATE LNDEYVSTEH LMVGLATGDS
DAAKLLQNAG AGPQALRDAF QAVRGTARVT SENPEDTYQS LEKYSTDLTK RARAGELDPV
IGRDSEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRVVEGDVPE SLRDKTVVSL
DLGAMVAGAK YRGEFEERLK AVLDEIKAAD GQIITFIDEL HTIVGAGATG DSAMDAGNMI
KPLLARGELR LVGATTLEEY RQYIEKDAAL ERRFQQVYVG EPSVEDTIGI LRGLKERYEV
HHGVRITDSA LVAAASLSDR YITSRFLPDK AIDLVDEAAS RLRMEIDSRP IEVDEIERIV
RRLEVEELAL EKESDDASKE RLDKLRGELA DQREKLNELT ARWQAEKNVL DSVRDVKEEL
ERLRGEADRA ERDGDLGRAA ELRYGTIPGL EKKLEEAVEK SGAEAGADGS IMPKEEVGPD
DVADVVSAWT GVPAGRMLEG ETAKLLRMES HIAQRVIGQE EAITAVSDAV RRARAGVADP
NRPLGSFMFL GPTGTGKTEL AKSLAEFLFD DEHAMVRIDM SEYGEKHSVA RLVGAPPGYV
GYDQGGQLTE AVRRRPYSVV LFDEVEKAHP DVFDVMLQVL DEGRLTDGQG RTVDFRNTIL
ILTSNLGAGG DRDQVMAAVR ARFKPEFINR LDDILIFEAL SPEQLVSIVD IQLRGLSDRL
AARRLTLDVS DEAKEWLGAR GYDPLYGARP LRRLIQQAIG DQLAKALLAG DIRDGDTVHV
TIDEATDSLK VG
//
