ID A0A139NF20_9STRE Unreviewed; 810 AA.
AC A0A139NF20;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:KXT74364.1};
GN ORFNames=STRDD10_00985 {ECO:0000313|EMBL:KXT74364.1};
OS Streptococcus sp. DD10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777878 {ECO:0000313|EMBL:KXT74364.1, ECO:0000313|Proteomes:UP000072050};
RN [1] {ECO:0000313|EMBL:KXT74364.1, ECO:0000313|Proteomes:UP000072050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD10 {ECO:0000313|EMBL:KXT74364.1,
RC ECO:0000313|Proteomes:UP000072050};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-2016) 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:KXT74364.1}.
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DR EMBL; LQRE01000081; KXT74364.1; -; Genomic_DNA.
DR RefSeq; WP_067193574.1; NZ_KQ969159.1.
DR AlphaFoldDB; A0A139NF20; -.
DR STRING; 1777878.STRDD10_00985; -.
DR PATRIC; fig|1777878.3.peg.1087; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000072050; 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; -; 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; 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:KXT74364.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KXT74364.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000072050};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 810 AA; 89828 MW; A6A2AA56319F53AE CRC64;
MKHSIALQDS LKGAQIFAGH FEGNYLETWH LLIAFSNNPY SVAGSSMSEF PLVLDRLENA
ASDITGKVYQ EDSFEQTRPF SKRLLHLFEE AEKIAGVVAA KEVGTEHVLF AIFMDRGNVA
LRILEEAGFG YSEEDEVKMA DLRSSLENKA GWTKENIKAL RMLHRGQTKS TNSMNQMLGM
PQTPSGGLDD YTRDLTDLAR QGILEPIIGR DEEISRMIQI LSRKTKNNPV LVGEAGVGKT
ALALGLAQRV ATGEVPAELA KMRVLELDLM SVVAGTRFRG DFEERMNNII KDIEEDGQVI
LFIDELHTIM GSGSGIDSTL DAANILKPAL ARGTLRTVGA TTQEEYQKHI EKDAALTRRF
AKVTIDEPTV KDSIAILQGL KESYETHHHV TITDQTIEVA VTYAHRYLTS RYLPDSAIDL
LDEAAATVQN RMKAGKISDD IFSPADYALL DAQWKQAGKL LSADEDTIVK KGIVEPEDIL
STLSRLSGIP VQKLSQTDAK KYLNLEAELH KRVIGQEQAV SSISRAIRRN QSGIRSHKRP
IGSFMFLGPT GVGKTELAKA LAEVLFDDES ALIRFDMSEY MEKFAASRLN GAPPGYVGYE
EGGELTEKVR NKPYSVLLFD EVEKAHPDIF NVLLQVLDDG VLTDSKGRKV DFSNTIIIMT
SNLGATALRD DKTVGFGAKD IRFDQENMEK RVFEVLKRAY RPEFLNRIDE KVVFHSLTAE
HMQEVVKIMV KPLISSLKTQ GVDLKFQPSA LKLLAEKGYD PEMGARPLRR TLQTQVEDQL
AELLLAGDLV AGQTIKVGVK AGRLKFDITN
//
