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Database: UniProt
Entry: L8DG14_9NOCA
LinkDB: L8DG14_9NOCA
Original site: L8DG14_9NOCA 
ID   L8DG14_9NOCA            Unreviewed;       801 AA.
AC   L8DG14;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574};
GN   ORFNames=RHODMAR_2192 {ECO:0000313|EMBL:CCQ15566.1};
OS   Rhodococcus sp. AW25M09.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ15566.1, ECO:0000313|Proteomes:UP000011207};
RN   [1] {ECO:0000313|EMBL:CCQ15566.1, ECO:0000313|Proteomes:UP000011207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ15566.1,
RC   ECO:0000313|Proteomes:UP000011207};
RA   Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA   Smalaas A.O., Altermark B.;
RT   "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT   from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL   Submitted (DEC-2012) 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:CCQ15566.1}.
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DR   EMBL; CAPS01000059; CCQ15566.1; -; Genomic_DNA.
DR   RefSeq; WP_008714552.1; NZ_CAPS01000059.1.
DR   AlphaFoldDB; L8DG14; -.
DR   STRING; 1268303.RHODMAR_2192; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000011207; Unassembled WGS sequence.
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: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   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   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};
KW   Hydrolase {ECO:0000313|EMBL:CCQ15566.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CCQ15566.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          15..159
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
SQ   SEQUENCE   801 AA;  87060 MW;  0A2BFF7D8BA98627 CRC64;
     MPAFLGPEGP RRIDISRLLS QSTQSLIGDA AMFAAGRGDR ELDALHVLHV MAQNDPTRSL
     MQRAGAQSPA VIDAVELRLP QSRSEAAVSA TALSSTLKTA ILEAHNIAQT LGSTYIDPEH
     LFLSFAADRE HIAGRLLGEE GITPEGLQTA LRGGSVEPES NSETPTLDKY GIDLTQRARE
     GGIDPVIGRT DEIQQTIEIL SRRTKNNPVL VCEAGVGKTA VVEGLAQRIV DGEVPERLSN
     KRIVQLDLSA IVAGTRYRGD FEERLTSVID EIVAHKDELI VFIDEVHSIA GAGGGADGAM
     DAGNILKPKL ARGELHIVGA TTLDEYRMNI EKDPALERRF QPVTVPEPSV PDAIAILTGL
     KSRYEQHHGV KYTDEAISAA VELADRYIGD RFLPDKAIDL IDQAGARKQL SLPSIDAEAI
     ATQLAAIDTD KSAAIASEDY ERASALRDEA AQLQMRLDGT VTDTPDVTAE DIAYVVSRST
     GIPASQMTTE EKERLLTLES ELHRRVVGQD EAVKAIARAV RRNRTGMNDP DRPVGSFLFL
     GPTGVGKTEL AKALAASLFG DQKKLLRLDM SEFGERHTVS RLLGAPPGYV GYGEAGQLTE
     QVRRNPYSVI LLDEIEKAHP DVFDTLLQVL DDGRLTDGQG RTVNFRNTVV IMTSNLGSDI
     ISSKSGGTGF ALGAADEKPM QDKVMGRLRE AMRPEFLNRI DEIVVFRKLD DAQLLRITDL
     MLQESRERLS ARGIEITFSD SAIDWLAHNG HQPEFGARPL RRAIQRSLDD KIADLLLDDI
     VTDGRTVSVD VTGDELSLNC A
//
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