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Database: UniProt
Entry: Q6APV8_DESPS
LinkDB: Q6APV8_DESPS
Original site: Q6APV8_DESPS 
ID   Q6APV8_DESPS            Unreviewed;       750 AA.
AC   Q6APV8;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   SubName: Full=Probable ATP-dependent Clp protease, ATP-binding subunit ClpA {ECO:0000313|EMBL:CAG35615.1};
GN   OrderedLocusNames=DP0886 {ECO:0000313|EMBL:CAG35615.1};
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG35615.1, ECO:0000313|Proteomes:UP000000602};
RN   [1] {ECO:0000313|Proteomes:UP000000602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CR522870; CAG35615.1; -; Genomic_DNA.
DR   RefSeq; WP_011188129.1; NC_006138.1.
DR   AlphaFoldDB; Q6APV8; -.
DR   STRING; 177439.DP0886; -.
DR   KEGG; dps:DP0886; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_7; -.
DR   OMA; GRVIQEH; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000000602; 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:CAG35615.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CAG35615.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000602};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..67
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
SQ   SEQUENCE   750 AA;  82834 MW;  2877437C0AC98FE7 CRC64;
     MISKTLEQSL VRALQEAKKR KHQFVTIEHM LYGLLADDLA CYIIKECGAS IDTLREKLDK
     FFETRVPKIS SSTEEEAVQT VAFNRVLQRA LNHVKSCGKK EADAGDILVA IFGEKDSHAV
     YFLTSLGLNR MAVVSFIAHD IPSDNQQESL NAPAKTPEET PGESALEKYT TNLTVNAAKG
     LIDPLIGRES ELKRIMQVLC RRKKNNPLLV GEPGVGKTAI VEGLARHIFE DSLARRDGRK
     TKFPELLHDT DIYLLDMGSL VAGTKYRGDF EKRLKAVISE IKEEENAILF IDEIHTIVGA
     GSTSEGSMDA SNLLKPALQE GVLRCIGSTT YEEYKSHIEK DRALSRRFQK IDLPEPSVAD
     TQLILQGVKS QYEKHHNIKY SDESILAMAE LADRYINERF LPDKAIDVMD EIGSRFRLAG
     RKKAIVRVKD VEEVVSEIAR IPAKQTSASE ANQLRHLDNS LRSVVYGQDN AIKALTTAVK
     RSRAGLGNPL SPTGSFVFSG PTGVGKTEVA RQLAKQLGIH FERFDMSEYM EKHAVARLIG
     APPGYVGFDQ GGQLTEAIRK HPHCVLLLDE IEKAHPDIFS ILLQVMDHAT LTDNSGRRAD
     FRNVILIMTS NAGAREMTTT PIGFVQDKTT KGKGAIKKLF APEFRNRLDA IIAFDQLSIK
     SAEKVVGKLL TEISAQLADK NVSISLTAGA KKYLASKGYS PEFGARPLQR LILTEIGDVL
     SDEILFGQLK NGGSVKIGCK NKALTFSYGK
//
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