ID A0A1X6X505_9MICO Unreviewed; 875 AA.
AC A0A1X6X505;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=FM110_10800 {ECO:0000313|EMBL:SLM93993.1};
OS Brachybacterium nesterenkovii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=47847 {ECO:0000313|EMBL:SLM93993.1, ECO:0000313|Proteomes:UP000195981};
RN [1] {ECO:0000313|EMBL:SLM93993.1, ECO:0000313|Proteomes:UP000195981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP104813 {ECO:0000313|EMBL:SLM93993.1,
RC ECO:0000313|Proteomes:UP000195981};
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; FWFG01000093; SLM93993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6X505; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000195981; 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:UP000195981};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 87..114
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 403..504
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 875 AA; 97245 MW; E772C0ADF6E62CA4 CRC64;
MDMNSLTQKS QEALTSAQSI AVQAGQIETD EEHLLLALLQ QEEGLVPRLL QTAGADVEAV
RADVEAEIAR KPSVSGSSPQ TGQVYVSRSL TSTLERAERE AKRLKDSYIS VEHLVLALVD
DSSNRPASRV LRGHGVTRES FLSALTKIRG NQHVNSATPE QTYEALAKYG RDLVADARLG
KLDPVIGRDA EIRRVIQILS RKTKNNPVLI GEPGVGKTAI VEGLAQRILS EDVPEGLRDK
TVFSLDLSAL VAGAKYRGEF EERMKAVLAE VKAAEGRILL FIDELHTLVG AGATEGAMDA
GNMLKPMLAR GELHLIGATT LDEYRKHIEK DAALERRFQT VMVEEPDVED AISILRGLRE
RLEVFHGVRI QDSALVAAAV LSHRYITDRF LPDKAIDLID EACARLRTEI DSMPAELDEL
TRRVTRLEIE EAALSKETDP ASKKRLEELR RELADLKAEA DSKRAQWEAE RQAIRKVQEL
RGELERLRRE AEEAERSYDL NRAAELRYGA IADVERRLRA EEERLTSKQG GQRLLREVVT
EDEIAEIVAA WTGIPVARLK EGERDKILSL EATLKERVVG QDEAITLVSD AIIRARSGIR
DPRRPIGSFI FLGPTGVGKT ELAKALAQAL FDSESAMVRL DMSEYQERHT VSRLVGAPPG
YVGYEEGGQL TEAVRRRPYS VVLFDEIEKA HPDVFNTLLQ VLDDGRITDS QGRTVDFRNT
ILIMTSNIGA HHLLGLDGGS IPDDVRNSVL GELRAHFRPE FLNRVDDIVV FSPLGREQIQ
DIVELQFNDL RSRLAERQIR IELTPAARQL IAERGYDPVY GARPLRRYIS HEIETRLGRA
LLSGQVMDGS TVTLDVQDGD LVFNIAAPAE EEDAG
//