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Database: UniProt
Entry: R5YN71_9FIRM
LinkDB: R5YN71_9FIRM
Original site: R5YN71_9FIRM 
ID   R5YN71_9FIRM            Unreviewed;       513 AA.
AC   R5YN71;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:CDA28315.1};
GN   ORFNames=BN504_01854 {ECO:0000313|EMBL:CDA28315.1};
OS   Eubacterium sp. CAG:156.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262880 {ECO:0000313|EMBL:CDA28315.1, ECO:0000313|Proteomes:UP000018124};
RN   [1] {ECO:0000313|EMBL:CDA28315.1, ECO:0000313|Proteomes:UP000018124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:156 {ECO:0000313|Proteomes:UP000018124};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDA28315.1}.
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DR   EMBL; CBBN010000027; CDA28315.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5YN71; -.
DR   STRING; 1262880.BN504_01854; -.
DR   Proteomes; UP000018124; 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:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion 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   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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:CDA28315.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:CDA28315.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:CDA28315.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018124};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          213..372
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          415..509
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  57355 MW;  709B963A35B53051 CRC64;
     MDKEFETKED MNIKENEEII NDKETTDESL DNTNETKKDY IKKEDTTSTD KDDNEDEDEK
     ICYVCRRPES RAGKMVSMPG NIYVCTDCLQ RSFDTMNDGL AGFPGFGGLN GMNVNISEED
     LEKLLKMPNV RMVTSDDFNR EIPKNQKLKK KKKTEEKEVK TIDLANLPAP HKIKEQLDEY
     VVGQDYAKKV MSVGVYNHYK RVANTIQDDV EIEKSNMLMI GPTGCGKTFL VKTLAKILDV
     PLAIADATSL TEAGYIGDDI ESVLSKLLAA ADNDVERAET GIVFIDEIDK LAKKQNSTNR
     DVSGESVQQG LLKLLEGSEV EVPVGATSKN AMVPLATVNT KNILFICGGA FPGLEDIIKE
     RLNKQATIGF MSDLKDKYDK DAKILSKVIN EDLRKFGMIP EFIGRLPIIF TLEGLTEEML
     VKILTEPKNA IIKQYKKLLA IDEVDLRFTE DALKEIAARA INKNTGARAL RSIIEDFMLD
     IMYEIPKDDN IGTVTVTKEC IEKKGAPIIG FRG
//
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