ID A0A2Z4UDB0_9FIRM Unreviewed; 475 AA.
AC A0A2Z4UDB0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:AWY98927.1};
GN ORFNames=DQQ01_13130 {ECO:0000313|EMBL:AWY98927.1};
OS Blautia argi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1912897 {ECO:0000313|EMBL:AWY98927.1, ECO:0000313|Proteomes:UP000250003};
RN [1] {ECO:0000313|Proteomes:UP000250003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 15426 {ECO:0000313|Proteomes:UP000250003};
RA Chang Y.-H., Paek J., Shin Y.;
RT "Description of Blautia argi sp. nov., a new anaerobic isolated from dog
RT feces.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP030280; AWY98927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4UDB0; -.
DR KEGG; blau:DQQ01_13130; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000250003; Chromosome.
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 Pfam; PF06689; zf-C4_ClpX; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:AWY98927.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:AWY98927.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:AWY98927.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000250003};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 166..327
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 368..463
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 53400 MW; B0C99D7D3568AB78 CRC64;
MSDDKEFLDT TNTSDTPGEK EHKDEYEKIC FMCRRPESKA GKMIDLPNDI HICTDCMQRS
FDTMNNTNIN YDELMKNMPN ISMIDLSSLQ NQIPQRQKVK KKQEQPKAKT APKVFDIKSI
PAPHKIKASL DEYVIGQEYA KKVMSVGVYN HYKRIFADIS DEVEIEKSNM LMIGPTGSGK
TYMVKTLARL LDVPLAITDA TSLTEAGYIG DDIESVVSKL LAAADNDVER AEHGIIFIDE
IDKIAKKKNT NQRDVSGEAV QQGMLKLLEG SEVEVPVGAN SKNAMVPLAT VNTKNILFIC
GGAFPDLEEI IKERLNKTAS IGFQADLKDK YDHDNKLLEK VTVDDLKKFG MIPEFLGRMP
IIFTLSGLDR DMLVEILKEP KNAILKQYQK LLALDEVKLE FEDGALEAIA DMAMEKHTGA
RALRAILEEY MLDIMYEIPK DDNIGEVIIT KDYITHTGGP RILLRGQEPA QIEMK
//
