ID V6Z2Z3_STRAG Unreviewed; 812 AA.
AC V6Z2Z3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=ATP-dependent Clp protease ATP-binding protein {ECO:0000313|EMBL:ESV55088.1};
GN ORFNames=SAG0136_07670 {ECO:0000313|EMBL:ESV55088.1};
OS Streptococcus agalactiae LMG 14747.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1154860 {ECO:0000313|EMBL:ESV55088.1, ECO:0000313|Proteomes:UP000018482};
RN [1] {ECO:0000313|EMBL:ESV55088.1, ECO:0000313|Proteomes:UP000018482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 14747 {ECO:0000313|EMBL:ESV55088.1,
RC ECO:0000313|Proteomes:UP000018482};
RA Richards V.P., Durkin S.A.S., Kim M., Pavinski Bitar P.D., Stanhope M.J.,
RA Town C.D., Venter J.C.;
RL Submitted (MAY-2013) 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:ESV55088.1}.
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DR EMBL; ANQC01000111; ESV55088.1; -; Genomic_DNA.
DR AlphaFoldDB; V6Z2Z3; -.
DR eggNOG; COG0542; Bacteria.
DR Proteomes; UP000018482; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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};
KW Hydrolase {ECO:0000313|EMBL:ESV55088.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ESV55088.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 812 AA; 90914 MW; 805323E5C58D4A62 CRC64;
MVKYSQKMQD VFGLSQMIAT QFSCQLLESW HLLLGLIVSD ETIAGLTFRE FDQEVNEQDY
FAATILATEK KYDDSVQRFD LYEQSAATME VLQFAEQISQ ITNDEEVGTE HVLMAILLSP
RLMPVRILEL AGFKAKNDGE GISLFNLRQS LEKHAGFTKD QVKAIHELKK PKRPKAGNFT
DMMKPPSTAG ELTDFTRDLT AMAQVGELET VVGRDKEISR MVQVLSRKTK NNPVLVGEAG
VGKTALAYGL AQRIVSGEIP YELRDMRVLE LDMMSVVAGT RFRGDFEERM NQIIDDIEAD
GHIILFVDEM HTIMGSGSGI DSTLDAANIL KPALSRGTLH MVGATTQEEY QKHIEKDAAL
SRRFAKILIE EPSVADTLEI LKGLRPSYEA YHHVSLSDEV LMSAVKAAHR YMTSKHLPDS
AIDLIDEASA TVQTMIKKEA QAELSSIDEA LLDQDMKTVT RLLKKEETLA LPKVVKVTEE
HILATLSRLT GIPVEKMTQT ENQKYLNLEK ELHKRVIGQE MAISAISRAI RRNQSGIRTG
KRPIGSFMFL GPTGVGKTEL AKALAEVLFD DESALIRFDM SEYMEKFAAS RLNGAPPGYV
GYEEGGELTE KVRQRPYSVL LFDEVEKAHP DIFNVLLQVL DDGVLTDSRG RKVDFSNTLI
IMTSNLGATA LRDDKTVGFG AQDLSRNHDA MEKRIFEELK KAYRPEFINR IDEKVVFHSL
SQEDMRQVVK IMVQPLIKQL AEKDIVLKIQ PSALKHLSEE GYDVEMGARP LRRTLQTHVE
DHLAELVLSG QVSAGHTLKI GMKQGKLKFE VT
//
