ID A0A2S0P7Q7_9NEIS Unreviewed; 769 AA.
AC A0A2S0P7Q7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:AVY93396.1};
GN Name=clpA {ECO:0000313|EMBL:AVY93396.1};
GN ORFNames=DAI18_04555 {ECO:0000313|EMBL:AVY93396.1};
OS Microvirgula aerodenitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Microvirgula.
OX NCBI_TaxID=57480 {ECO:0000313|EMBL:AVY93396.1, ECO:0000313|Proteomes:UP000244173};
RN [1] {ECO:0000313|EMBL:AVY93396.1, ECO:0000313|Proteomes:UP000244173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BE2.4 {ECO:0000313|EMBL:AVY93396.1,
RC ECO:0000313|Proteomes:UP000244173};
RA Anderson E., Jang J., Ishii S.;
RT "Denitrifier Microvirgula.";
RL Submitted (APR-2018) 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 -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP028519; AVY93396.1; -; Genomic_DNA.
DR RefSeq; WP_028498119.1; NZ_CP028519.1.
DR AlphaFoldDB; A0A2S0P7Q7; -.
DR STRING; 1122240.GCA_000620105_00652; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000244173; Chromosome.
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:AVY93396.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AVY93396.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244173};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 142..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 84023 MW; 2076380FB38209FD CRC64;
MIAQELEVSL HMAFMEARQK RHELISVEHL LLAMLDNPSA AEVLRACNAN IDQLRRQLAE
FIDQHTPTVP GTEDVETQPT LGFQRVIQRA ILHVQSSGKK EVTGANILVA IFGEKDSHAV
YFLHQQNISR LDVVNYISHG ITKNKSSDAT PARGAAAPAP EGEAEQEAEA TAAGGALENY
TQNLNQLAQA GKVDPLIGRD HELERVIQIL CRRRKNNPLL VGEAGVGKTA IAEGLARRIV
RGEVPDVLSQ ATVYSLDMGA LLAGTKYRGD FEQRLKAVIK QLADDPHAIL FIDEIHTLIG
AGAASGGTLD ASNLLKPALS NGSMRCIGAT TYTEYRGIFE KDNALSRRFQ KIDVVEPTVE
QTIQILKGLK SRFESHHGVK YTVAALTSAA ELAARYITDR HLPDKAIDVI DEAGAAQKIL
PKSRQKKVIS KHEIEEIISK IARIPAKTVS NDDRNALRTL DRDLKNVVFG QDQAIDALAA
AIKMSRSGLG NPQKPIGSFL FSGPTGVGKT EVARQLAYTL GIELIRFDMS EYMERHAVSR
LIGAPPGYVG FEQGGLMTEA ISKHPYSVLL LDEIEKAHPD IFNVLLQVMD HGTLTDNNGR
KADFRNVIII LTTNAGAENL SKGSIGFTST KAAGDEMADI KRLFTPEFRN RLDAIISFKT
LNEDIILQVV DKFLIQLEAQ LAEKKVEVHF TEPLKKHLAS KGFDPLMGAR PMARLIQDTI
RKVLADELLF GRLADGGSVT VDLDQEGGVV LLFDEPETKK PQPAPAAAI
//
