ID K0NHE2_DESTT Unreviewed; 581 AA.
AC K0NHE2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=ClpX: ATP-dependent Clp protease, ATP binding subunit {ECO:0000313|EMBL:CCK80370.1};
GN Name=clpX {ECO:0000313|EMBL:CCK80370.1};
GN OrderedLocusNames=TOL2_C22090 {ECO:0000313|EMBL:CCK80370.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK80370.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK80370.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
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DR EMBL; FO203503; CCK80370.1; -; Genomic_DNA.
DR RefSeq; WP_014957682.1; NC_018645.1.
DR AlphaFoldDB; K0NHE2; -.
DR STRING; 651182.TOL2_C22090; -.
DR KEGG; dto:TOL2_C22090; -.
DR PATRIC; fig|651182.5.peg.2615; -.
DR HOGENOM; CLU_014218_7_0_7; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 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; 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; 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 Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:CCK80370.1};
KW Protease {ECO:0000313|EMBL:CCK80370.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT DOMAIN 113..226
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 324..416
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 581 AA; 65657 MW; 3D28D7D997D7C5CC CRC64;
MTDKKNIRSQ DPKKIEKELG EFLNKKFGGN VKIISPSVLP HQEPISGKPA DNRRKNLINF
NIKPEELIAY LDQYVVRQAK AKSVLATKIC THFNRIRHSQ TSGEEMSKIT GNIKSNILML
GPTGIGKTYL IKLIAKKIGV PFVKADATKF SETGYVGGDV EDLIRDLVKD ANDDIALAEC
GIVYIDEIDK IAASPNVIGA QVSRTGVQRA LLKPMEETDV DLKVPHDPVS MMQELEAYQR
TGKRSRRRVN TSNILFIVSG AFGGLSDVIR TRLSKQNIGF GSKLVKSQND NDLLNKTKAE
DLVNFGFESE FIGRIPVRCI LDPLSEEDLF SILKMPNNPV TLSKRLDFNA YGIKIVFTDD
ALKFLAQKAS KENTGARGLV SAVEEALLDF EEKLPSHNIC KFAVTKKVLE DPKNHLNDLI
SKQNLATWDM LYEKAFLDHK TYISSYIKDN WKTFSIGHGL NLSESLCNMM ALCFCNTVME
IEDAVKKIKK LHDSVKEIEL EVSKSYNLNI VFEEDAIDFL IEQFIKHNAT SEEILTKIYD
NYYDGFNLIR EKTGKNRFFL TKKALVDHET YLNDLIRKEI I
//
