ID A0A3Q8WVM4_9ACTO Unreviewed; 869 AA.
AC A0A3Q8WVM4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:AZN30145.1};
GN ORFNames=EJO69_07355 {ECO:0000313|EMBL:AZN30145.1};
OS Flaviflexus salsibiostraticola.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Flaviflexus.
OX NCBI_TaxID=1282737 {ECO:0000313|EMBL:AZN30145.1, ECO:0000313|Proteomes:UP000270021};
RN [1] {ECO:0000313|EMBL:AZN30145.1, ECO:0000313|Proteomes:UP000270021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 33148 {ECO:0000313|EMBL:AZN30145.1,
RC ECO:0000313|Proteomes:UP000270021};
RA Bae J.-W.;
RT "Complete genome sequence of Flaviflexus salsibiostraticola KCTC 33148.";
RL Submitted (DEC-2018) 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; CP034438; AZN30145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q8WVM4; -.
DR KEGG; fsl:EJO69_07355; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000270021; Chromosome.
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:UP000270021};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 405..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 94578 MW; 13012F75977324E7 CRC64;
MDKLTTKSQE AISSALEMAV RAGNPQLEPI HLLAALLGQN EGVAIGMLDA IGVDRGALNQ
RVQATLTALP GAQGSSVAQP AASRPFSLVL SDAGKEATAL GDAYVSTEHL LMGLAASQSS
AGDILRSAGA GRDQLQDVLG QVRGSRRVDS PDPEGTYDAL EKYGQDLTQI ARDGKLDPVI
GRDTEIRRVV QVLSRRTKNN PVLIGEPGVG KTAVVEGLAQ RIVDGDVPES LRGKRLIALD
IAAMVAGAKY RGEFEERLKA VLQEIKDSDG EIVTFIDELH TVVGAGRGSD GSMDAGNMLK
PMLARGELRL VGATTLDEYR ENIEKDPALE RRFQQIFVGE PSVDDTVAIL RGIAPKYEAH
HKVTISDGAL VAAAELSDRY ISGRQLPDKA IDLVDEAASR LRMELDSSPE EIDTLQRQVD
RLKMEESYLV DTLGDDTDAE RLDKIRSELA DRSEELAALN ARWENEKAGR NRVGDLKVRL
DELRTELERA IREGRYEDAG RIQNGDIPEV EQRIAEGEAD ESPDDGLEPM IAEHVDADEI
AQVVAAWTGI PVGRLLATET EKLLHMEDVI GQRLVGQKEA VASVSDAVRR SRAGIADPNR
PTGSFLFLGP TGVGKTELAK SLADFLFDDE RAMIRIDMSE YSEKHSVARL VGAPPGYVGY
EEGGQLTEAV RRRPYAVVLL DEVEKAHPEV FDILLQVLDD GRLTDGQGRT VDFRNVILIL
TSNLGSQFLA DPTLSEEEKR AAVDRTVQGA FKPEFLNRLD DIVYFRPLGM SEIASIVELQ
VAHLAQRLQS RRITLDVTPR ARDYLAVEGY DPAYGARPLR RLIQREIGDE LARLILAGTV
SDGDTVMVDS PEDLGQGMTL TVVSTEPVA
//