ID A0A2K5XK75_MANLE Unreviewed; 648 AA.
AC A0A2K5XK75;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit B {ECO:0000313|Ensembl:ENSMLEP00000003698.1};
GN Name=CLPB {ECO:0000313|Ensembl:ENSMLEP00000003698.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000003698.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000003698.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_011849050.1; XM_011993660.1.
DR AlphaFoldDB; A0A2K5XK75; -.
DR Ensembl; ENSMLET00000017699.1; ENSMLEP00000003698.1; ENSMLEG00000015735.1.
DR GeneID; 105549229; -.
DR CTD; 81570; -.
DR GeneTree; ENSGT00390000012961; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF93; CASEINOLYTIC PEPTIDASE B PROTEIN HOMOLOG; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT REPEAT 133..169
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 206..238
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 314..468
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 512..601
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 51..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 72487 MW; 9899EA9B6B1474AC CRC64;
MLGSLVLRRK ALAPRLLLRL LRSPTLRGHG GASGRNVTTG SLGEPQWLRA AAGGRPGTSP
ALFSGRGAAT GGRQGGRFDT KCLAAATWGR LLGPEETLPG QDSWNGVPNR ARLGMWALAT
ALVVHCYSKS PSNKDAALLE AARANNVQEV TSVVQVLLAA GADPNLGDDF SSVYKTAKEQ
GIHSLEVLIT REDDFNNRLN NRASFKGCTA LHYAVLADDY RTVKELLDGG ANPLQRNEMG
HTPLDYAREG EVMKLLRTSE TKYQEKQRKR EAEERRRFPL EQRLKEHIIG QESAIATVGA
AIRRKENGWY DEEHPLVFLF LGSSGIGKTE LAKQTAKYMH KDAKKGFIRL DMSEFQERHE
VAKFIGSPPG YVGHEEGGQL TKKLKQCPNA VVLFDEVDKA HPDVLTIMLQ LFDEGRLTDG
KGKTIDCKDA IFIMTSNVAS DEIAQHALQL RQEALEMSRN RIAENLGDVQ ISDKITISKN
FKENVIRPIL KAHFRRDEFL GRINEIVYFL PFCHSELIQL VNKELNFWAK RAKQRHNITL
LWDREVADVL VDGYNVHYGA RSIKHEVERR VVNQLAAAYE QDLLPGGCTL RITVEDSDKQ
LLKSPELPSP QTEKRLPKLR LEIIDKDSKT RKLDIRAPLH PEKVCNTI
//