ID A0A1R1I3U1_9ACTN Unreviewed; 856 AA.
AC A0A1R1I3U1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BJN44_11855 {ECO:0000313|EMBL:OMG53395.1};
OS Tessaracoccus sp. ZS01.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1906324 {ECO:0000313|EMBL:OMG53395.1, ECO:0000313|Proteomes:UP000187142};
RN [1] {ECO:0000313|EMBL:OMG53395.1, ECO:0000313|Proteomes:UP000187142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS01 {ECO:0000313|EMBL:OMG53395.1,
RC ECO:0000313|Proteomes:UP000187142};
RA Salah Z., Rout S.P., Humphreys P.N.;
RT "Range of isolates obtained from hyperalkaline sediments.";
RL Submitted (OCT-2016) 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}.
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:OMG53395.1}.
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DR EMBL; MTHC01000015; OMG53395.1; -; Genomic_DNA.
DR RefSeq; WP_076063172.1; NZ_PQFE01000015.1.
DR AlphaFoldDB; A0A1R1I3U1; -.
DR STRING; 1906324.BJN44_11855; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000187142; 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:UP000187142};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 253..280
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 436..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 856 AA; 93130 MW; E61016ED6532A2FA CRC64;
MNTERLTTKS RDAVTAAVRQ ALTNGNPNTE PVHLLHGLLL TPDNTVGALL EAVGAGAAQV
DAAAVAAIKK LPSTSGSSVS QPALSGPFAR VLAAAETLAD SLGDDFVATE HLLIGLATVA
SDAKTILDNA GVTADALKTS FEASRGGKRV TSAESEGGES VLEKYSIDLT ERARSGKLDP
VIGRDQEIRR VVQVLARRTK NNPVLIGEPG VGKTAVVEGL AQRLVAGDVP DSLKGRRLVS
LDLASMVAGA KYRGEFEERL KAVLNEIKEA EGQIVTFIDE LHTVVGAGAS GEGAMDAGNM
LKPMLARGEL RMIGATTLDE YRERIEKDPA LERRFQQVYV GEPSVDDTVA ILRGLRERYE
AHHKVRITDS ALVAAAELSN RYITSRQLPD KAIDLVDEAA SRLRMEIDSS PEEIDMLRRD
VDRMTMQKFH LEKEDDEASR ERLAALNAEL ADAQEKLRGL ELRWESEKSG LNRVGDLKER
IDQLRMEADR AQREGDLTKA STILYGEIPA AEKELAEAEA SDATPSMVSE EVSAADIAEV
VAAWTGVPVG RLLQGESEKL LQMEERLGER LIGQRSAVVA VSDAVRRSRA GISDPNRPTG
SFLFLGPTGV GKTELAKALA DFLFDDETAL VRIDMSEYSE KHSVARLVGA PPGYVGYEEG
GQLTEAVRRR PYSVILLDEV EKAHPDLFNI LLQVLDDGRL TDGQGRTVDF RNTLLIMTSN
LGSQFMADPL LDREEKEKSV MSVVRQAFRP EFLNRLDEVV LFDALTREQL SQIVDIQLRR
LNARLASRRI AVEVSDAAKL WLGEAGFDPV YGARPLRRLV QSTIEDDLAR GLLSGAINDG
QTVRFDRTDD GIGIVS
//