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Database: UniProt
Entry: A0A117M452_9BACT
LinkDB: A0A117M452_9BACT
Original site: A0A117M452_9BACT 
ID   A0A117M452_9BACT        Unreviewed;       858 AA.
AC   A0A117M452;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Chaperone ClpB 1 {ECO:0000313|EMBL:KUK83349.1};
GN   ORFNames=XD98_0367 {ECO:0000313|EMBL:KUK83349.1};
OS   Microgenomates bacterium 39_6.
OC   Bacteria; Candidatus Microgenomates.
OX   NCBI_TaxID=1641391 {ECO:0000313|EMBL:KUK83349.1, ECO:0000313|Proteomes:UP000053541};
RN   [1] {ECO:0000313|Proteomes:UP000053541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(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:KUK83349.1}.
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DR   EMBL; LGGT01000047; KUK83349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117M452; -.
DR   PATRIC; fig|1641391.3.peg.355; -.
DR   Proteomes; UP000053541; 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..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..497
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   858 AA;  96611 MW;  509DE4816913918F CRC64;
     MLKPEKFTVK AQQVISESQD LAKNNHQPSL EPLHILAALL ADNESIVVTT LNQNKIDVDK
     LKNQVQEAIK NLPQVGTESD QIYASPQTIK VLNQAEKEMA SFKDGYISSE HLFLALLSVD
     SQAKELLVKN GLQKSQIIKT FQDQRQGQKA DSPSAEGKYQ ALEKFTINLN DLAQEGSLDP
     VIGRDQEIRR IMEILSRRRK NNPVLLGDPG VGKTAIVEGL AQRIISGDVP ELLKNKEIIS
     LDLAAMLAGA KFRGEFEERL KAVISSIEKA GGRYILFIDE LHTLVGAGSA EGAVDASNML
     KPALARGTLH AIGATTVKEY RQHIEKDAAL ERRFQPIMIE EPSKEDSLAI LRGLKEKYQL
     HHGVRISDQA LVAAIDLSSR YISDRFLPDK AIDLVDEAAA ALSIEIQSVP QKIDNLRRSL
     RQTQIELAAV KKEKNKDRIQ KLEKNIADME EKLRALENKW DQQKEILAKI KKTRQKLEKL
     SLEEEQAEQE VDLEKAAQIK YGQIPQTEKE LKEALAQWDK IPEEEKIIKQ EVDEEQVAQV
     VSRWTGIPIA RLVESEAQKL AKLEEEIHKR LVNQEEAVVE VANAIRRNRA GIGEQNKPIG
     VFLFLGPTGV GKTELAKTLA YILFNDESAM VRIDMSEYQE RHTVARLIGS PPGYIGHEEG
     GQLTEAIRRK PYSVILFDEI EKAHPDVFNL FLQIFDDGRL TDSQGRTVDF QNTIIIMTSN
     LGSDIIQKEE NKKTIEEKIT QLIEKTFRPE FINRLDQIVL FEKLTKDQIG QIVDLQLQKV
     KKNLAKNKKL TLQISPKAKE LIADLGYDPQ YGARSLKRVI QNNILDKIAL LIVNGKIKEG
     QTVKVEATQK NTFQITPR
//
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