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Database: UniProt
Entry: A0A174GI54_9FIRM
LinkDB: A0A174GI54_9FIRM
Original site: A0A174GI54_9FIRM 
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
//
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