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Database: UniProt
Entry: A0A417CVN6_9FIRM
LinkDB: A0A417CVN6_9FIRM
Original site: A0A417CVN6_9FIRM 
ID   A0A417CVN6_9FIRM        Unreviewed;       477 AA.
AC   A0A417CVN6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:RHS99801.1};
GN   ORFNames=DW904_09230 {ECO:0000313|EMBL:RHS99801.1};
OS   Ruminococcus sp. AM42-11.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=2292372 {ECO:0000313|EMBL:RHS99801.1, ECO:0000313|Proteomes:UP000284976};
RN   [1] {ECO:0000313|EMBL:RHS99801.1, ECO:0000313|Proteomes:UP000284976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM42-11 {ECO:0000313|EMBL:RHS99801.1,
RC   ECO:0000313|Proteomes:UP000284976};
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   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01250}.
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:RHS99801.1}.
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DR   EMBL; QUIO01000013; RHS99801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A417CVN6; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000284976; 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; 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   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:RHS99801.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:RHS99801.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:RHS99801.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284976};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT   DOMAIN          22..76
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         37
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"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ   SEQUENCE   477 AA;  53425 MW;  811BA79475250AA6 CRC64;
     MTEHFDDEKD EIIDGDITEK NDDHEDDSDY EKFCFLCHRP ESQAGKMIEL PNNIHICNDC
     MQKSFDTMTQ QMNNGLNLND LLNMPNVSMI NLGSIQDAIP RPKKVKKKKE DARPEIDLKK
     IPAPHKIKAS LDEYVIGQER AKKVMSVAVY NHYKRVATDT MDEIEIEKSN MLMIGPTGCG
     KTYLVKTLAR LLDVPLAIAD ATSLTEAGYI GDDIESVISK LLAAADNDVE KAEHGIVFID
     EIDKLAKKKN TNQRDVSGEA VQQGLLKLLE GSEVEVPVGA NSKNAMVPMV TVNTRNILFI
     CGGAFPDLEN IIKERLNKQA SIGFYADLKD KYDNDPHILE KVTVDDIRAF GMIPEFIGRL
     PIIYTLDGLN EDMLVQILKE PKNAILKQYQ KLLALDEVKL DYEEDALHAI AAKALEKHTG
     ARGLRAILEE YMLDIMYEIP KDDSIGQVII TREYIEGTGG PRILLRGQEI PLIGMAQ
//
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