ID A0A3R6VSJ1_9CLOT Unreviewed; 482 AA.
AC A0A3R6VSJ1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:RHU81108.1};
GN ORFNames=DXC26_13100 {ECO:0000313|EMBL:RHU81108.1};
OS Clostridiaceae bacterium OM08-6BH.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae.
OX NCBI_TaxID=2292274 {ECO:0000313|EMBL:RHU81108.1, ECO:0000313|Proteomes:UP000284832};
RN [1] {ECO:0000313|EMBL:RHU81108.1, ECO:0000313|Proteomes:UP000284832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM08-6BH {ECO:0000313|EMBL:RHU81108.1,
RC ECO:0000313|Proteomes:UP000284832};
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:RHU81108.1}.
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DR EMBL; QUKV01000008; RHU81108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R6VSJ1; -.
DR Proteomes; UP000284832; 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; IPR000641; CbxX/CfxQ.
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 PRINTS; PR00819; CBXCFQXSUPER.
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:RHU81108.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:RHU81108.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:RHU81108.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000284832};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 175..336
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 482 AA; 54002 MW; DA5E3F2D961A9D62 CRC64;
MDNEKDFREI DENGVELSDV KETEIHEEHP VDEYEDVCFI CHRPESKAGK MIHLTPEIHI
CAECMQRTMD MMNNGNVDYN KMDFSRMPNI SMINLSDLQN MIPKRQKVKK KNPEKEAEAQ
KMFDIHAIPA PHKIKASLDE YVVGQEKAKK VISVAVYNHY KRVAAGSDAD GIEIEKSNML
MIGPTGSGKT YLVKTLARLL DVPLAIADAT SLTEAGYIGD DIESVLSKLL AAADNDVEKA
ERGIVFIDEI DKIAKKKNTN QRDVSGESVQ QGLLKLLEGA DVEVPVGANS KNAMVPLETM
NTKNILFICG GAFPDLEEII KERLNKQSSI GFRADLKDKY DNDKNLIRQV TVEDLRNFGM
IPEFLGRLPV IYTLDALSEE MMVKILKEPK NAILKQYQKL LALDEVKLEF TDDALTAIAR
KAMEKDTGAR ALRAIIEDFM LDIMYEIPKD DNIGRVTITA DYINHKGGPL ITMRGVPALE
GE
//