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Database: UniProt
Entry: A0A2Y9K401_ENHLU
LinkDB: A0A2Y9K401_ENHLU
Original site: A0A2Y9K401_ENHLU 
ID   A0A2Y9K401_ENHLU        Unreviewed;       619 AA.
AC   A0A2Y9K401;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial isoform X2 {ECO:0000313|RefSeq:XP_022368001.1};
GN   Name=LOC111153328 {ECO:0000313|RefSeq:XP_022368001.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022368001.1};
RN   [1] {ECO:0000313|RefSeq:XP_022368001.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022368001.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_022368001.1; XM_022512293.1.
DR   AlphaFoldDB; A0A2Y9K401; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840,
KW   ECO:0000313|RefSeq:XP_022368001.1};
KW   Hydrolase {ECO:0000313|RefSeq:XP_022368001.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|RefSeq:XP_022368001.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          93..146
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          68..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..599
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  67393 MW;  08E9BB4AEA38CE96 CRC64;
     MSGCGACTCG TAAARLISSS LASAQRGISC GRIHIPVLGR LGTFETQILR RAPFRTFTET
     PAYFASKDGI SKDGSGDGNK KSASEGSSKK SGSGNSGKGG NQLRCPKCGD LCTHVETFVS
     STRFVKCEKC HHFFVVLSEA DSKKSIIKEP ESAAEAVKLA FQQKPPPPPK KIYNYLDKYV
     VGQSFAKKVL SVAVYNHYKR IYNNIPANLR QQAEVEKQTS LTPRELLQIA GISPHGNALG
     ASMQQQVNQQ IPQEKRGGEV LDSSHDDIKL EKSNILLLGP TGSGKTLLAQ TLAKCLDVPF
     AICDCTTLTQ AGYVGEDIES VIAKLLQDAN YNVEKAQQGI VFLDEVDKIG SVPGIHQLRD
     VGGEGVQQGL LKLLEGTIVN VPEKNSRKLR GETVQVDTTN ILFVASGAFN GLDRIISRRK
     NEKYLGFGTP SNLGKGRRAA AAADLANRSG ESNTHQDIEE KDRLLRHVEA RDLIEFGMIP
     EFVGRLPVVV PLHSLDEKTL VQILTEPRNA VIPQYQALFS MDKCELNVTE DALKAIARLA
     LERKTGARGL RSIMEKLLLE PMFEVPNSDI VCVEVDKEVV EGKKEPGYIR APTKESSEEE
     YDSGVEEEGW PRQADAANS
//
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