ID   CLPB_RAT                Reviewed;         677 AA.
AC   Q9WTT2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Caseinolytic peptidase B protein homolog;
DE            EC=3.6.1.- {ECO:0000250|UniProtKB:Q9H078};
DE   AltName: Full=Suppressor of potassium transport defect 3;
DE   Flags: Precursor;
GN   Name=Clpb; Synonyms=Skd3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Testis;
RA   Hondo E.;
RT   "Molecular cloning and expression of suppressor of potassium transport
RT   defect 3 (SKD3) in rat testis.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function as a regulatory ATPase and be related to
CC       secretion/protein trafficking process. Involved in mitochondrial-
CC       mediated antiviral innate immunity, activates RIG-I-mediated signal
CC       transduction and production of IFNB1 and pro-inflammatory cytokine IL6.
CC       {ECO:0000250|UniProtKB:Q9H078}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9H078};
CC   -!- SUBUNIT: Interacts with PHB and PHB2. Interacts with MAVS; the
CC       interaction is enhanced by Sendai virus infection.
CC       {ECO:0000250|UniProtKB:Q9H078}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:Q9H078}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; AB027570; BAA78095.1; -; mRNA.
DR   RefSeq; NP_075236.1; NM_022947.1.
DR   AlphaFoldDB; Q9WTT2; -.
DR   SMR; Q9WTT2; -.
DR   STRING; 10116.ENSRNOP00000026665; -.
DR   iPTMnet; Q9WTT2; -.
DR   PhosphoSitePlus; Q9WTT2; -.
DR   jPOST; Q9WTT2; -.
DR   PaxDb; Q9WTT2; -.
DR   PRIDE; Q9WTT2; -.
DR   GeneID; 65041; -.
DR   KEGG; rno:65041; -.
DR   CTD; 81570; -.
DR   RGD; 621328; Clpb.
DR   eggNOG; KOG1051; Eukaryota.
DR   InParanoid; Q9WTT2; -.
DR   PhylomeDB; Q9WTT2; -.
DR   PRO; PR:Q9WTT2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140374; P:antiviral innate immune response; ISO:RGD.
DR   GO; GO:0034605; P:cellular response to heat; ISO:RGD.
DR   GO; GO:0039529; P:RIG-I signaling pathway; ISO:RGD.
DR   Gene3D; 1.25.40.20; -; 2.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13857; Ank_5; 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; SSF48403; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
PE   2: Evidence at transcript level;
KW   Acetylation; ANK repeat; ATP-binding; Hydrolase; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..677
FT                   /note="Caseinolytic peptidase B protein homolog"
FT                   /id="PRO_0000191241"
FT   REPEAT          133..162
FT                   /note="ANK 1"
FT   REPEAT          166..195
FT                   /note="ANK 2"
FT   REPEAT          235..265
FT                   /note="ANK 3"
FT   REPEAT          268..297
FT                   /note="ANK 4"
FT   REGION          64..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         351..358
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         559
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H078"
SQ   SEQUENCE   677 AA;  75702 MW;  C386466154D5C739 CRC64;
     MMLSAVLRRT APAPRLFLGL IKSPSLQSRG GAYNRSVITG DRGEPQRLRT AAWVRPGASS
     VLFPGRGAAT GGRRGERTEI PYLTAASSGR GPSPEETLPG QDSWNGVPNK AGLGMWALAM
     ALVVQCYNKN PSNKDAALME AARANNVQEV RRLLSEGADV NARHKLGWTA LMVAAISHNE
     SVVQVLLAAG ADPNLGDDFS SVYKTANEQG VHSLEVLVTR EDDFNNRLNH RASFKGCTAL
     HYAVLADDYS IVKELLGGGA NPLQRNEMGH TPLDYAREGE VMKLLKTSET KYMEKQRKRE
     AEERRRFPLE QRLEQHIIGQ ESAIATVGAA IRRKENGWYD EEHPLVFLFL GSSGIGKTEL
     AKQTAKYMHK DAKKGFIRLD MSEFQERHEV AKFIGSPPGY IGHEEGGQLT KKLKQCPNAV
     VLFDEVDKAH PDVLTIMLQL FDEGRLTDGK GKTIDCKDAI FIMTSNVASD EIAQHALQLR
     QEALEMSRNR IAENLGDVQI SDKITISKNF KENMIRPILK AHFRRDEFLG RINEIVYFLP
     FCHSELIQLV NKELNFWAKR AKQRHNITLL WDREVADVLV DGYNVQYGAR SIKHEVERRV
     VNQLAAAYEQ DLLPGGCTLR ITVEDSDKQL LKSPELPSPQ AEKRPPTLRL EIIDKDSKTH
     KLDIQAPLHP EKVCYTI