ID C1CBH2_STRP7 Unreviewed; 810 AA.
AC C1CBH2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=ClpB protein {ECO:0000313|EMBL:ACO17651.1};
GN Name=clpB {ECO:0000313|EMBL:ACO17651.1};
GN OrderedLocusNames=SP70585_2322 {ECO:0000313|EMBL:ACO17651.1};
OS Streptococcus pneumoniae (strain 70585).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488221 {ECO:0000313|EMBL:ACO17651.1, ECO:0000313|Proteomes:UP000002211};
RN [1] {ECO:0000313|Proteomes:UP000002211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70585 {ECO:0000313|Proteomes:UP000002211};
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP000918; ACO17651.1; -; Genomic_DNA.
DR RefSeq; WP_001109692.1; NC_012468.1.
DR AlphaFoldDB; C1CBH2; -.
DR KEGG; snm:SP70585_2322; -.
DR HOGENOM; CLU_005070_4_1_9; -.
DR Proteomes; UP000002211; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
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 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; 1.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 810 AA; 90163 MW; AC2AA5F787B1FC65 CRC64;
MNYSKALNEC IESAYMVAGH FGARYLESWH LLIAMSNHSY SVAGATLNDY PYEMDRLEEV
ALELTETDYS QDETFTELPF SRRLQVLFDE AEYVASVVHA KVLGTEHVLY AILHDGNALA
TRILERAGFS YEDKKDQVKI AALRRNLEER AGWTREDLKA LRQRHRTVAD KQNSMAHMMG
MPQTPSGGLE DYTHDLTEQA RSGKLEPVIG RDKEISRMIQ ILSRKTKNNP VLVGDAGVGK
TALALGLAQR IASGDVPAEM AKMRVLELDL MNVVAGTRFR GDFEERMNNI IKDIEEDGQV
ILFIDELHTI MGSGSGIDST LDAANILKPA LARGTLRTVG ATTQEEYQKH IEKDAALSRR
FAKVTIEEPS VADSMTILQG LKATYEKHHR VQITDEAVET AVKMAHRYLT SRHLPDSAID
LLDEAAATVQ NKANHVKADD SDLSPADKAL MDGKWKQAAQ LIAKEEEVPV YKDLVTESDI
LTTLSRLSGI PVQKLTQTDA KKYLNLEAEL HKRVIGQDQA VSSISRAIRR NQSGIRSHKR
PIGSFMFLGP TGVGKTELAK ALAEVLFDDE SALIRFDMSE YMEKFAASRL NGAPPGYVGY
EEGGELTEKV RNKPYSVLLF DEVEKAHPDI FNVLLQVLDD GVLTDSKGRK VDFSNTIIIM
TSNLGATALR DDKTVGFGAK DIRFDQENME KRMFEELKKA YRPEFINRID EKVVFHSLSS
DHMQEVVKIM VKPLVASLAE KGIDLKLQAS ALKLLANQGY DPEMGARPLR RTLQTEVEDK
LAELLLKGDL VAGSTLKIGV KAGQLKFDIA
//
