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Database: UniProt
Entry: A0A1T5DYE1_9FIRM
LinkDB: A0A1T5DYE1_9FIRM
Original site: A0A1T5DYE1_9FIRM 
ID   A0A1T5DYE1_9FIRM        Unreviewed;       544 AA.
AC   A0A1T5DYE1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:SKB76635.1};
GN   ORFNames=SAMN06296386_10539 {ECO:0000313|EMBL:SKB76635.1};
OS   Lachnospiraceae bacterium.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1898203 {ECO:0000313|EMBL:SKB76635.1, ECO:0000313|Proteomes:UP000191179};
RN   [1] {ECO:0000313|EMBL:SKB76635.1, ECO:0000313|Proteomes:UP000191179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH1P17 {ECO:0000313|EMBL:SKB76635.1,
RC   ECO:0000313|Proteomes:UP000191179};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FUZG01000005; SKB76635.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5DYE1; -.
DR   Proteomes; UP000191179; 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; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
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   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:0000313|EMBL:SKB76635.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:SKB76635.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:SKB76635.1};
KW   Protease {ECO:0000313|EMBL:SKB76635.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191179}.
FT   DOMAIN          222..383
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          424..518
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          83..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  60115 MW;  2914B8E873C34EB9 CRC64;
     MSDNKDEKNT KTEVEICTVC RRPDTVAGKM LHFPNNMNIC NDCMQRFMDQ IGSLDLGTLS
     QLSGMPMDYS SFMAGLDQAA AQGAVEKAES EDVTIEKKED GEPVEAKDKK EPDTENPEKK
     ETSGKKSGGF GIPGFPNIQF LNLGDFGGPM QGQTGKVHKS SKEDIEKEFD FHKIPKPHAL
     KKMLDEYVIG QDHAKKVVSV AVYNHFKRIN AEVSGKNKSE IDKSNILLLG PTGCGKTYLV
     QTLAKLLQVP LAIADATSLT EAGYIGDDIE SVVSKLLAAA DNDVERAERG IIFIDEIDKI
     AKKKNSTSRD VSGESVQQGM LKLLEGAEVE VPVGANSKNA MVPMVKVNTR NILFICGGAF
     PDLDELIRAR LRKETSIGFN AELKDHWDKE KDILKKVTTE DLRSFGMIPE FLGRLPITCP
     MEGLTEDSMV RILREPKNAI IRQYEDLLEM DEVQLRFTDD ALHAIAAKAM KRDTGARALR
     SIIEAFMLDI MFEVPKDDNI GRVTITKEFV EGSGGPVIDL RGVAELEAEQ VSKIEEKKED
     AVNE
//
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