ID A0A417U6J2_9FIRM Unreviewed; 492 AA.
AC A0A417U6J2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:RHV49024.1};
GN ORFNames=DXB46_08595 {ECO:0000313|EMBL:RHV49024.1};
OS Lachnospiraceae bacterium OM04-12BH.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=2292272 {ECO:0000313|EMBL:RHV49024.1, ECO:0000313|Proteomes:UP000284430};
RN [1] {ECO:0000313|EMBL:RHV49024.1, ECO:0000313|Proteomes:UP000284430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM04-12BH {ECO:0000313|EMBL:RHV49024.1,
RC ECO:0000313|Proteomes:UP000284430};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RHV49024.1}.
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DR EMBL; QULQ01000007; RHV49024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417U6J2; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000284430; 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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein 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 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:RHV49024.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:RHV49024.1};
KW Nucleotide-binding {ECO:0000313|EMBL:RHV49024.1};
KW Protease {ECO:0000313|EMBL:RHV49024.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000284430}.
FT DOMAIN 175..335
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 377..472
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 492 AA; 54999 MW; 495191826F94A5D4 CRC64;
MADFDEKDKD QKDTLTEDQK ESDYEDVCFI CRRPESKAGK MFKLPNNICV CNDCMHKTMD
TVSQFDYQGM LDPNFMNSLN QDMSKKGFPN IRFLNIADLQ GEGGIPNKQK IKKKKKSEGT
EPVLDIRNIP PPHRIKAQLD DYVIGQEHAK KVISVAVYNH YKRVATGTMD DIEIEKSNML
MIGPTGCGKT YLVKTLARLL DVPLAITDAT SLTEAGYIGD DIESVVSKLL AAADNDVEKA
ERGIIFIDEI DKIAKKKNTT SRDVSGESVQ QGMLRLLEGA EVEVPVGANS KNAMVPLTTI
NTRNILFICG GAFPDLEEII KQRLRRQTSI GFNAELKDKY DNDTDILSKV TIEDLKKFGM
IPEFLGRLPI IYTLKALDKD MMVRILKEPK NAILKQYQKL LELDEVQLCF DDGALEAIAE
KAMKKDIGAR ALRAIIEDFM LDIMYEIPKD DNIGKVTITR EYIEGAGGPV IDIRNSAAIS
ADGLKAIEAQ EK
//