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Database: UniProt
Entry: R4KJV5_9FIRM
LinkDB: R4KJV5_9FIRM
Original site: R4KJV5_9FIRM 
ID   R4KJV5_9FIRM            Unreviewed;       815 AA.
AC   R4KJV5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:AGK99910.1};
GN   ORFNames=Desgi_0328 {ECO:0000313|EMBL:AGK99910.1};
OS   Desulfoscipio gibsoniae DSM 7213.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=767817 {ECO:0000313|EMBL:AGK99910.1, ECO:0000313|Proteomes:UP000013520};
RN   [1] {ECO:0000313|EMBL:AGK99910.1, ECO:0000313|Proteomes:UP000013520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7213 {ECO:0000313|EMBL:AGK99910.1,
RC   ECO:0000313|Proteomes:UP000013520};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA   Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA   Brambilla E., Spring S., Stams A.F., Woyke T.;
RT   "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP003273; AGK99910.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4KJV5; -.
DR   STRING; 767817.Desgi_0328; -.
DR   KEGG; dgi:Desgi_0328; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   Proteomes; UP000013520; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   Gene3D; 4.10.860.10; UVR domain; 1.
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   InterPro; IPR001943; UVR_dom.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 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.
DR   PROSITE; PS50151; UVR; 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|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013520};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          424..459
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          420..466
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   815 AA;  90297 MW;  81E49C6B1D996823 CRC64;
     MLFGRFTQRA QKVLMLAQEE AKRFNHPYVG TEHILLGLIS EGEGVAAKAL ASLGVQADKV
     RAMVEQSIGQ GEGTPREMAL TPRVKRVLEL SVDEARRMGT NYVGTEHLLL GLIREGEGVA
     AQVLGALDVN QERVRQIVIQ LLGGAGGMSQ GQQPQPGCAG GACGTKTATL DQYGRDLTSM
     AREDNLDPVV GREKEIERVV QILSRRTKNN PVLIGDPGVG KTAVVEGLAQ RIVAGNVPEI
     LLQKRLVTLD LASLVAGTKY RGEFEERLKK VVEEITREKD VIVFIDELHT IIGAGAAEGA
     IDAANILKPA LARGELQCIG ATTLDEYRKH IERDSALERR FQPITVEEPS VEETVQILTG
     LRDKYEAHHR VRITDDALKA AARLSDRYIT DRFLPDKAID LMDEAGSRVR LQAFTAPPDV
     KDLEQRIEEI CKEKEAAVNN QEFEKAAQLR DEESKLRQEL DGKRSTWQQQ KGGKKLEVTA
     EDIAQIVASW TGIPVKKLAE EESDRLLRME EILHQRVVGQ DEAVAAVSRA IRRARAGLKD
     PKRPIGSFIF LGPTGVGKTE LARALAEAMF GDEDAMVRID MSEYMEKFAV SRLVGAPPGY
     VGYDEGGQLT DAVRRKPYSV VLLDEIEKAH PDVFNILLQV LEDGRLTDAK GRTVDFRNTV
     IIMTSNVGVG LIKRETTMGF KTNEGANTSY ENMKKRVMDD LRRAFRPEFL NRIDDIIVFH
     GLSQVHIKEI VGLMVQEVAG RLAENEIAIE VTDAAGEYLA REGFDEEYGA RPLRRAIQKE
     IEDRLSEEML RGTFRRGDRV LIDKETGGGL KVVKI
//
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