ID A0A174GI54_9FIRM Unreviewed; 476 AA.
AC A0A174GI54;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:CUO62073.1};
GN Name=clpX_2 {ECO:0000313|EMBL:CUO62073.1};
GN ORFNames=ERS852394_02611 {ECO:0000313|EMBL:CUO62073.1},
GN ROSSTS7063_02165 {ECO:0000313|EMBL:VUX12379.1};
OS Blautia obeum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=40520 {ECO:0000313|EMBL:CUO62073.1, ECO:0000313|Proteomes:UP000095409};
RN [1] {ECO:0000313|EMBL:CUO62073.1, ECO:0000313|Proteomes:UP000095409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608837 {ECO:0000313|EMBL:CUO62073.1,
RC ECO:0000313|Proteomes:UP000095409};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VUX12379.1, ECO:0000313|Proteomes:UP000409147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ruminococcus_obeum_SSTS_Bg7063 {ECO:0000313|EMBL:VUX12379.1};
RA Hibberd C M., Gehrig L. J., Chang H.-W., Venkatesh S.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC ProRule:PRU01250}.
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DR EMBL; CYZD01000016; CUO62073.1; -; Genomic_DNA.
DR EMBL; CABHNB010000030; VUX12379.1; -; Genomic_DNA.
DR RefSeq; WP_055066502.1; NZ_CYZD01000016.1.
DR AlphaFoldDB; A0A174GI54; -.
DR Proteomes; UP000095409; Unassembled WGS sequence.
DR Proteomes; UP000409147; 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:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 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 InterPro; IPR038366; Znf_CppX_C4_sf.
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 SMART; SM00994; zf-C4_ClpX; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:CUO62073.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:CUO62073.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:CUO62073.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095409};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT DOMAIN 17..73
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ SEQUENCE 476 AA; 53287 MW; 74FADB1FCE1E23F7 CRC64;
MADKYEDEIL EGEVSDDDDQ EENKKEPEKY CTLCHRAESQ VGKMIDLPNN IHICPDCMQR
SFDSMNQQMQ TGNFNYGDLL NMPNVSMIDL SSFQNQMGQQ KKPKKKKAEK KEPVLDLKKI
PAPHKIKATL DEYVIGQEYA KKVMSVAVYN HYKRVATDTM DEIAIEKSNM LMIGPTGCGK
TYLVKTLAKL LDVPLAIADA TSLTEAGYIG DDIESVVSKL LAAADNDVEK AEHGIIFIDE
IDKIAKKKNT NQRDVSGEAV QQGMLKLLEG ADVEVPIGAN SKNAMVPLTT VNTRNILFIC
GGAFPDLENI IKERLNKQAS IGFYADLKDK YDDDPHILEK VTVEDLRSFG MIPEFIGRLP
IIFTMNGLTE DMMVQILSEP RNAILKQYQK LLALDEVKLE FEEGALHAIA TKAMEKHTGA
RALRAILEEY MLDIMYEIPK DDNIGQVTIT REYIEGNGGP KILLRGQEVP LLEGNH
//