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Database: UniProt
Entry: A0A1X6X505_9MICO
LinkDB: A0A1X6X505_9MICO
Original site: A0A1X6X505_9MICO 
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
//
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