ID A0A367FMI9_9ACTN Unreviewed; 872 AA.
AC A0A367FMI9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RCG31613.1};
GN ORFNames=DQ384_08590 {ECO:0000313|EMBL:RCG31613.1};
OS Sphaerisporangium album.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sphaerisporangium.
OX NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG31613.1, ECO:0000313|Proteomes:UP000253094};
RN [1] {ECO:0000313|EMBL:RCG31613.1, ECO:0000313|Proteomes:UP000253094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG31613.1,
RC ECO:0000313|Proteomes:UP000253094};
RA Li L.;
RT "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT the South China Sea.";
RL Submitted (JUN-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}.
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:RCG31613.1}.
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DR EMBL; QOIL01000004; RCG31613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367FMI9; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000253094; 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:UP000253094};
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 410..504
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 97496 MW; A7D8DFFA88B096A8 CRC64;
MDPNRLTQKS QEALHDAQTK AIRFGHTEVD GEHLLLALLE QPEGLVPRLI MAMGGDPDKL
RLELTAELER RPRVSGPGAA PGQVYVTQRL SRLLDTADAE AKRLKDEYIS VEHLLLALVE
EGPETAAGRL LNGQGLTRDS LLEALTRIRG NQRVTSATPE VAYEALEKYG RDLVADARAD
KLDPVIGRDT EIRRVMQILS RKSKNNPVLI GDPGVGKTAI VEGLAQRIAR GDVPEGLKDK
TIFMLDMGAL IAGAKYRGEF EERLKAVLTE VKASEGRILL FIDEVHNVVG AGATEGAMDA
GNMLKPMLAR GELHLIGATT VAEYRKYIEK DAALERRFQP VFVDEPSVED AISILRGLRE
RFEVFHGVKI QDGAIVAAVV MSHRYISDRF LPDKAIDLVD EACAMLRTEI DSMPAELDEL
TRRVMRLEIE EAALSKEDDP ASRQRLESLR RELADLRAEA DAMRAQWEAE RHALKKVQHL
RQEIEAVRRE AEQAERMYDL NRAAELMHGR LPELQHKLAL AEEQLQSKQG GHRLLREVVT
EDEIAGIVSR WTGIPITRLK EGEREKLLKL DEVLHERVIG QDEAVQAVTD AIIRARSGIK
DPRRPIGSFI FLGPTGVGKT ELAKALAEAL FDTEENMVRV DMSEYQERHT VSRLVGAPPG
YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HSDVFNTLLQ VLDDGRLTDA QGRTVDFRNT
VIIMTSNIGS HYLIDAVTPA GEIEPEARDL VMAELRSRFR PEFLNRVDDT VLFKPLTEPE
IEKIVSLMFN DIRKRLADRQ MTLDVTEAAL RHIAEQGFDP VYGARPLRRF IAREVETRIG
RALIAGDVRD GAVIRVDVVD GHLTVSYDNP AE
//