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
//