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Database: UniProt
Entry: A0A2S5W7F0_9MICO
LinkDB: A0A2S5W7F0_9MICO
Original site: A0A2S5W7F0_9MICO 
ID   A0A2S5W7F0_9MICO        Unreviewed;       721 AA.
AC   A0A2S5W7F0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=ATP-dependent chaperone ClpB {ECO:0000313|EMBL:PPF89750.1};
GN   ORFNames=C5B96_00645 {ECO:0000313|EMBL:PPF89750.1};
OS   Subtercola sp. Z020.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Subtercola.
OX   NCBI_TaxID=2080582 {ECO:0000313|EMBL:PPF89750.1, ECO:0000313|Proteomes:UP000238959};
RN   [1] {ECO:0000313|EMBL:PPF89750.1, ECO:0000313|Proteomes:UP000238959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z020 {ECO:0000313|EMBL:PPF89750.1,
RC   ECO:0000313|Proteomes:UP000238959};
RA   Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA   Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA   Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA   Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT   "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT   US Biological Select Agent, Rathayibacter toxicus.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:PPF89750.1}.
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DR   EMBL; PSTT01000007; PPF89750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5W7F0; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000238959; 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; 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; 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; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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}.
FT   DOMAIN          53..198
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          454..622
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          621..712
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          267..347
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   721 AA;  79430 MW;  BA2339E9DF86064A CRC64;
     MQPQSGQQNV DEQSALEKYG VNLTKIAASG KLDPVIGRDA EIRRVSQVLT RRTKNNPVLI
     GEPGVGKTAV VEGLAQRIVA GDVADSLKGK QLVSLDLAAL VAGAKYRGEF EERLKAVLQE
     INDADGEIIT FVDELHTLMG AGGGEGSVAA SNMLKPMLAR GELRLIGATT LNEYREYIEK
     DAALERRFQQ VFVGEPSVED TIAILRGLKE RYEAHHKVAI ADAALVAAAS LSNRYISGRQ
     LPDKAIDLID EAASRLRMEI DSAPVEIDEL RRSVDRLRLE ELALKKEKDD ASKQRLEKLR
     DDLATRSADL EVLQERWDRE RAVLNRVGEL KTQLDAARMS AEKAQREGNL ERASKLLYGE
     IPVIERQLRE AESAEQYPDG ERMVSDQVTE AEIAAVIAAW TGIPVDRLTQ GETQKLLNLE
     KELGKRLIGQ RPAVRAVADA VRRTRAGISD PNRPTGSFLF LGPTGVGKTE LAKALAEFLF
     DDERAMIRID MSEYGEKHSV ARLLGAPPGY IGYEQGGQLT EAVRRRPYSV VLMDEVEKAH
     PEVFDVLLQV LDDGRLTDGQ GRTVDFRNTI LILTSNLGSQ FLVDPTLSDD AKEAAVLQVV
     RQAFKPEFVN RLDDIVVFTA LTHDDLAQIV SLYVDRLARR VSERGLSLAV TPDARSWLAD
     KGYDPAYGAR PLRRLMQREI DDRLSMALLS GAIRDGDTVY VGLDPDGTAL TVGPVVLVPE
     D
//
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