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Database: UniProt
Entry: R5GLR2_9BACT
LinkDB: R5GLR2_9BACT
Original site: R5GLR2_9BACT 
ID   R5GLR2_9BACT            Unreviewed;       107 AA.
AC   R5GLR2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:CCY16649.1};
GN   ORFNames=BN773_00723 {ECO:0000313|EMBL:CCY16649.1};
OS   Prevotella sp. CAG:755.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262935 {ECO:0000313|EMBL:CCY16649.1, ECO:0000313|Proteomes:UP000018353};
RN   [1] {ECO:0000313|EMBL:CCY16649.1, ECO:0000313|Proteomes:UP000018353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:755 {ECO:0000313|Proteomes:UP000018353};
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:CCY16649.1}.
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DR   EMBL; CAXR010000190; CCY16649.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5GLR2; -.
DR   STRING; 1262935.BN773_00723; -.
DR   Proteomes; UP000018353; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
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; PF10431; ClpB_D2-small; 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:CCY16649.1};
KW   Hydrolase {ECO:0000313|EMBL:CCY16649.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:CCY16649.1};
KW   Protease {ECO:0000313|EMBL:CCY16649.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018353}.
FT   DOMAIN          8..99
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   107 AA;  12267 MW;  59DFCB510AD55EC5 CRC64;
     MLTYLSPLDR HALRNILTEP KNSIIKQYVK LFAMDGVTLT FAPETLDYIV DKAVEYKLGA
     RGLRSIVESV MIDAMFESPS AQRKEFTVTL DYAKRQLEKS RQQTAHD
//
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