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Database: UniProt
Entry: A0A0G1VJ53_9BACT
LinkDB: A0A0G1VJ53_9BACT
Original site: A0A0G1VJ53_9BACT 
ID   A0A0G1VJ53_9BACT        Unreviewed;       902 AA.
AC   A0A0G1VJ53;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=ATP-dependent chaperone ClpB {ECO:0000313|EMBL:KKU78273.1};
GN   ORFNames=UY03_C0001G0011 {ECO:0000313|EMBL:KKU78273.1};
OS   Parcubacteria group bacterium GW2011_GWA2_47_64.
OC   Bacteria.
OX   NCBI_TaxID=1618845 {ECO:0000313|EMBL:KKU78273.1, ECO:0000313|Proteomes:UP000034132};
RN   [1] {ECO:0000313|EMBL:KKU78273.1, ECO:0000313|Proteomes:UP000034132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKU78273.1}.
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DR   EMBL; LCOL01000001; KKU78273.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1VJ53; -.
DR   PATRIC; fig|1618845.3.peg.12; -.
DR   Proteomes; UP000034132; Unassembled WGS sequence.
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; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 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.
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|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          4..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          415..538
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   902 AA;  100997 MW;  BB7DF3AE2AF48C01 CRC64;
     MPPFHHFTTK AKEAIRRAHE LAIERGQNHV NPLHLLAALM LQEESIVISI LERLEVDTVL
     LTDSILESIE GAEGSSVLSP SYQIYLTPEL AQTLESGSRV AATLKDEFVS TEHLFIAMFD
     VSGSARELLA RFKLEKDSVL RVLDELRHSR VADASVSPKK FRFLAKFTRN LTSLARTNKL
     DPVIGRDSEI SRIIQILSRR TKNNPILIGE AGVGKTAIVE GLALRMSQGD IPESLKDKEL
     VSLDLGLLIA GTKYRGEFEE RLKNIMKEIE KSDGRIILFV DEIHTIVGAG AAEGAMDASN
     MLKPALSRGE LRAIGATTLK EYQKHIEKDP ALTRRFQTVF VPEPSVEDAI AILRGLKEKY
     ELYHGVHITD EAIVAAVNLS ARYITDRFLP DKAVDLIDEA ASSLKISLEN MPPVLEETRR
     KVMRLEIERE ALKQDSFASK QAKTRVKEIE TEIADLKEKT EEIELKWKNE KETLSEIKKS
     KKELETLRIE AEQAEARADL SKAAEIRYGK IPTLQKELEN NAKRLKKLQS SRRILKEEIL
     SNDIAEIVAK WTGIPVTRML EEETAKLARI EDELRRRIVG QDDPVKRVSD AIKRSRAGIS
     DPNRPIGSFL FLGPTGVGKT ELTKALAEFM FNDERALIRV DMSEFMERHS VSKLIGAPPG
     YVGHEEGGTL TETIRHRPYA VVLFDEIEKA HPEVFNILLQ ILDDGRLTDA KGRFANFRNA
     IIILTSNIGG QFIDKMQRVG FSVSGKAGDY DDAKNKVMTA LKDHFRPEFL NRLDDIVIFD
     ILGHEAIQKI VGIQIKQVEE RLKVKGIGIQ IAPEVYGYLS KEGYNPQYGA RPLKRLIQSK
     ILNPIASLII GKGIGEGGTV SLTMKNSDIH FEVRKGRNGK NGHAKPIKSD FVSEPVEARR
     GV
//
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