ID A0A553ZN01_9ACTN Unreviewed; 877 AA.
AC A0A553ZN01;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-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:TSB42837.1};
GN ORFNames=FNZ23_07700 {ECO:0000313|EMBL:TSB42837.1};
OS Streptomyces benahoarensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2595054 {ECO:0000313|EMBL:TSB42837.1, ECO:0000313|Proteomes:UP000320888};
RN [1] {ECO:0000313|EMBL:TSB42837.1, ECO:0000313|Proteomes:UP000320888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ03-48 {ECO:0000313|EMBL:TSB42837.1,
RC ECO:0000313|Proteomes:UP000320888};
RA Gonzalez-Pimentel J.L.;
RT "Draft genome for Streptomyces benahoarensis MZ03-48.";
RL Submitted (JUL-2019) 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:TSB42837.1}.
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DR EMBL; VKLS01000055; TSB42837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553ZN01; -.
DR Proteomes; UP000320888; 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:UP000320888};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 416..530
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 877 AA; 95327 MW; D4801C63749F526F CRC64;
MDAELTNKSR EALSAANERA ITAGHADMTS AHLLLALLAG PADSNANIID LLAAVGADAA
VLRGGAERRL AALPSVQGST VAPPQPDREL LAVLADAARR AKELGDAYVS TEHLLIGIAA
KGGATGALLD EQGASAKKLL AAFEESRGDR RVTNADPEGT YKALEKFGTD FTAAAREGKL
DPVIGRDHEI RRVVQVLSRR TKNNPVLIGE PGVGKTAVVE GLAQRIVKGD VPESLRNKRL
VALDLGAMVA GAKYRGEFEE RLKTVLAEIK SSDGQIITFI DELHTVVGAG AGGDSAMDAG
NMLKPMLARG ELRMVGATTL DEYRERIEKD PALERRFQQV LVAEPTVEDT VAILRGLKGR
YEAHHKVAIA DSALVAAATL SDRYITSRFL PDKAIDLVDE AASRLRMEID SSPVEIDELQ
RSVDRLKMEE LALRNETDAG SVARLEKLRR DLADKEEELR GLTARWEKEK QSLNRVGELK
ERLDDLRGQA ERAQRDGDFD TASKLLYGEI PKLEQELEAA AAAEAEQEAS AESMVKEEVG
PDDIADVVGA WTGIPAGRLL EGETQKLLRM EDELGKRLIG QGEAVRAVSD AVRRTRAGIA
DPDRPTGSFL FLGPTGVGKT ELAKALADFL FDDERAMVRI DMSEYGEKHS VARLVGAPPG
YVGYEEGGQL TEAIRRRPYS VVLLDEVEKA HHEVFDVLLQ VLDDGRLTDG QGRTVDFRNT
ILILTSNLGS NFLMDPLLKE EQKKEKVLET VRASFRPEFL NRLDDLVVFH PLGTDQLQRI
ARIQIDHLQK RLADRRLTLD ISDAALTWLA WLGQEPVVDA PAPDLSYGAR PLRRLVQTAI
GDQLARAILA GDVLDGDTVR VDVDGDHLAV TSARAAA
//
