ID F9HPW1_STRMT Unreviewed; 810 AA.
AC F9HPW1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Chaperone protein ClpB {ECO:0000313|EMBL:EGP65376.1};
GN Name=clpB {ECO:0000313|EMBL:EGP65376.1};
GN ORFNames=HMPREF9957_0706 {ECO:0000313|EMBL:EGP65376.1};
OS Streptococcus mitis SK1080.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1008453 {ECO:0000313|EMBL:EGP65376.1, ECO:0000313|Proteomes:UP000004568};
RN [1] {ECO:0000313|EMBL:EGP65376.1, ECO:0000313|Proteomes:UP000004568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1080 {ECO:0000313|EMBL:EGP65376.1,
RC ECO:0000313|Proteomes:UP000004568};
RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (MAY-2011) 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. 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}.
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:EGP65376.1}.
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DR EMBL; AFQV01000029; EGP65376.1; -; Genomic_DNA.
DR RefSeq; WP_001109665.1; NZ_AFQV01000029.1.
DR AlphaFoldDB; F9HPW1; -.
DR PATRIC; fig|1008453.3.peg.1705; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000004568; Unassembled WGS sequence.
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; 90234 MW; B5F5C3FDCDDCCB88 CRC64;
MNYSKALNEC IESAYMVAGH FGARYLESWH LLIAMSNHSY SVAGATLNDY PYEMDRLEEV
ALELTETDYS QDETFTELPF SHRLQVLFDE AEYVASVVHA KVLGTEHLLY AILHDGNALA
TRILERAGFS YEDKKDQVKI AALRRNLEER AGWTREDLKA LRQRHRTVAD KQNSMANMMG
MPQTPSGGLE DYTHDLTEQA RSGKLEPVIG RDKEISRMIQ ILSRKTKNNP VLVGDAGVGK
TALALGLAQR IASGDVPVEM AKMRVLELDL MNVVAGTRFR GDFEERMNNI IKDIEEDGQV
ILFIDELHTI MGSGSGIDST LDAANILKPA LARGTLRTVG ATTQEEYQKH IEKDAALSRR
FAKVTIEEPS VADSMTILQG LKATYEKHHR VQITDEAVET AVKMAHRYLT SRHLPDSAID
LLDEAAATVQ NKAKHVKADD FGLSPADKAL MDGKWKQAAQ LIAKEEEVPI YKDLVTESDI
LTTLSRLSGI PVQKLTQTDA KKYLNLEAEL HKRVIGQNQA VSSISRAIRR NQSGIRSHKR
PIGSFMFLGP TGVGKTELAK ALAEVLFDDE SALIRFDMSE YMEKFAASRL NGAPPGYVGY
EEGGELTEKV RNKPYSVLLF DEVEKAHPDI FNVLLQVLDD GVLTDSKGRK VDFSNTIIIM
TSNLGATALR DDKTVGFGAK DIRFDQENME KRMFEELKKA YRPEFINRID EKVVFHSLSS
DHMQEVVKIM VKPLVASLAE KGIDLKLQAS ALKLLANKGY DPEMGARPLR RTLQTEVEDK
LAELLLKGEL VAGSTLKIGV KAGQLKFDIV
//
