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Database: UniProt
Entry: R6TM81_9FIRM
LinkDB: R6TM81_9FIRM
Original site: R6TM81_9FIRM 
ID   R6TM81_9FIRM            Unreviewed;       476 AA.
AC   R6TM81;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:CDC59812.1};
GN   ORFNames=BN586_00826 {ECO:0000313|EMBL:CDC59812.1};
OS   Dorea formicigenerans CAG:28.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=1263073 {ECO:0000313|EMBL:CDC59812.1, ECO:0000313|Proteomes:UP000018109};
RN   [1] {ECO:0000313|EMBL:CDC59812.1, ECO:0000313|Proteomes:UP000018109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:28 {ECO:0000313|Proteomes:UP000018109};
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:CDC59812.1}.
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DR   EMBL; CBFN010000238; CDC59812.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6TM81; -.
DR   Proteomes; UP000018109; 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:CDC59812.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:CDC59812.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:CDC59812.1};
KW   Protease {ECO:0000313|EMBL:CDC59812.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018109}.
FT   DOMAIN          166..325
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          368..463
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  52994 MW;  CED182B4447BD1F9 CRC64;
     MSEQDYVDTI DNNDNNSNDN HNDDEYEKVC FVCHRPESVA GKMINLPNNM CVCNDCMQKS
     FDAMNNMNFG GAIDYSQLMN MPGVQFLNID DMSQQIPKQQ RVKKKKEGEE ATPLVDIHNL
     PAPHKIKASL DEYVVGQEYA KKVMSVAVYN HYKRVATDSM DDIEIEKSNM LMIGPTGSGK
     TYLVKTLARI LDVPLAITDA TSLTEAGYIG DDIESVVSKL LAAADNDVEK AEQGIIFIDE
     IDKIAKKKNA SQRDVSGESV QQGMLKLLEG SEVEVPVGAN SKNAMVPLTT VNTKNILFIC
     GGAFPDLDGI IKERLTKQSA IGFGADLKDK YDHDKKILEK VTTEDLRNFG MIPEFLGRLP
     VVFTLQGLTE DMYVKILEEP KNAILKQYQK LLALDEVKLD FTEDALRAIA KKAMEKDTGA
     RALRAIIEEF MLDIMYEIPK DDSIGQVTIT QEYIENTGGP IITLRGQEVP RLESQA
//
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