ID S6A9S8_SULDS Unreviewed; 754 AA.
AC S6A9S8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:BAN34635.1};
DE EC=3.4.21.92 {ECO:0000313|EMBL:BAN34635.1};
GN ORFNames=SCD_n00794 {ECO:0000313|EMBL:BAN34635.1};
OS Sulfuricella denitrificans (strain DSM 22764 / NBRC 105220 / skB26).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuricella.
OX NCBI_TaxID=1163617 {ECO:0000313|EMBL:BAN34635.1, ECO:0000313|Proteomes:UP000015559};
RN [1] {ECO:0000313|EMBL:BAN34635.1, ECO:0000313|Proteomes:UP000015559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skB26 {ECO:0000313|Proteomes:UP000015559};
RX PubMed=22773644; DOI=10.1128/AEM.01349-12;
RA Watanabe T., Kojima H., Fukui M.;
RT "Draft genome sequence of a psychrotolerant sulfur-oxidizing bacterium,
RT Sulfuricella denitrificans skB26, and proteomic insights into cold
RT adaptation.";
RL Appl. Environ. Microbiol. 78:6545-6549(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; AP013066; BAN34635.1; -; Genomic_DNA.
DR RefSeq; WP_009206418.1; NC_022357.1.
DR AlphaFoldDB; S6A9S8; -.
DR STRING; 1163617.SCD_n00794; -.
DR KEGG; sdr:SCD_n00794; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000015559; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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:BAN34635.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:BAN34635.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015559};
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 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 82962 MW; 63F38DBF78F9A0C5 CRC64;
MIAQELEVSL HMAFMEARQK RHEFITVEHL LLAMLDNPSA AKVLRACAAN IDELRKTLAD
FVTTQTPTIA GSGEVDTQPT LGFQRVIQRA ILHVQSSGKK EVTGANVLVA IFGEKDSHAV
YFLSQQGISR FDIVNYISHG ISKVPEGNAP RQDPEQESEQ ESAPAGALEN FTLNLNVHAL
AGKIDPLIGR ELELERTIQT LCRRRKNNPL LVGEAGVGKT AIAEGLARRI VEGEVPEVLA
ESTVYSLDMG ALLAGTKYRG DFEQRLKAVL KQLNDDPHAI LFIDEIHTLI GAGAASGGTL
DASNLLKPAL SSGQLRCIGA TTYNEYRGIF EKDHALSRRF QKIDVPEPSV EETVAILRGL
KSRFEAHHGV KYTATALTTA AELSARYIND RHLPDKAIDV IDEAGAAQRI LPKSKQKKTI
TNKEIEEIIA KIARIPPKNI SSDDRSALKT LDRDLKSVVF GQDKSIDMLA SAIKMARSGL
GNPHKPIGSF LFSGPTGVGK TEVARQLAYT LGIELIRFDM SEYMERHAVS RLIGAPPGYV
GFEQGGLLTE QITKHPYAVL LLDEIEKAHP DIFNILLQVM DHGTLTDNNG RKADFRNVII
IMTTNAGAES LTKSNIGFTT ARQQGDEMAE IKRLFSPEFR NRLDGTISFA PLSREVILRV
VDKFLMQLDE QLHEKKVDAV FTDALKDHLA KHGFDPAMGA RPMARLIQDT IRKALADELL
FGRLAHGGKV VVDIDEQEKV RLEFAENNEK AVSV
//