ID B6BWI4_9PROT Unreviewed; 750 AA.
AC B6BWI4;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 13-SEP-2023, entry version 77.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:EDZ64622.1};
GN Name=clpA {ECO:0000313|EMBL:EDZ64622.1};
GN ORFNames=KB13_754 {ECO:0000313|EMBL:EDZ64622.1};
OS beta proteobacterium KB13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OM43 clade.
OX NCBI_TaxID=314607 {ECO:0000313|EMBL:EDZ64622.1, ECO:0000313|Proteomes:UP000004188};
RN [1] {ECO:0000313|Proteomes:UP000004188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB13 {ECO:0000313|Proteomes:UP000004188};
RX PubMed=22675594; DOI=10.4056/sigs.2305090;
RA Huggett M.J., Hayakawa D.H., Rappe M.S.;
RT "Genome sequence of strain HIMB624, a cultured representative from the OM43
RT clade of marine Betaproteobacteria.";
RL Stand. Genomic Sci. 6:11-20(2012).
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 -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; DS995299; EDZ64622.1; -; Genomic_DNA.
DR AlphaFoldDB; B6BWI4; -.
DR STRING; 314607.KB13_754; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_4; -.
DR Proteomes; UP000004188; 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:0043335; P:protein unfolding; IEA:InterPro.
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; IPR013461; ClpA.
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; TIGR02639; ClpA; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 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 Hydrolase {ECO:0000313|EMBL:EDZ64622.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EDZ64622.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..133
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 750 AA; 83155 MW; B0B563B8603E9F94 CRC64;
MAFMDARQKR HELITVEHLL VAMLDNPSAQ EVLKACGANF DSLKKDLLNH IEEHTPIVNG
ENEVDTQPTL GFQRVIQRAM LHVQSSGKKE VTGANVLVAI FGEKDSHAVY FLHQQGIARL
DVVNFIAHGI EKELDKENEA DEVDEKIDQK TQNKESDLES YALNLNKVVL DGKIDPVIGR
ENEIERVAQI LCRRRKNNPL LVGDAGVGKT AIAEGLAKKI VDGDIPEVLK DTAIYSLDLG
ALIAGTKYRG DFEQRLKNVL KQLSKKPNAI LFIDEIHTII GAGSASGGTL DASNLLKPAL
AKGELRCIGA TTFNEYRTVF EKDHALTRRF QKIDVDEPSI PVSIEILKGL KKSFESHHKI
KFLNNALISA VELSAKYITD RKLPDKAIDV IDEAGALQKI LPKTKQKKTI SSKEIEEVIS
KIAKIPSKNI NQDDLSMLRN LDRDLKAIIF GQDEAINKLS TAIKMARSGL LSDNKPIGSF
MFSGPTGVGK TEVAKQLAYT LGIELIRIDM SEFMERHAVS KLIGAPPGYV GFDQGGTLTE
SINKNPYAVL LLDEIEKAHP DVHNILLQIM DNGFLTDSNG RKIDFRNVTL IMTTNVGAES
LSKSSLGFIA DDQTVFDEKK EINKAFSPEF RNRIDAIVSF APLENETILK VVDKFLIQLE
NQLHDKKVEV TFSDNLKNYL AKNGFDIKMG ARPMSRLIQD TIRKALADEL LFGKLVNGGD
VHIDIDENEN IKLQIESKQL TSSKKSLTSS
//
