ID A0A1H8VCE1_9GAMM Unreviewed; 393 AA.
AC A0A1H8VCE1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:SEP12991.1};
GN ORFNames=SAMN04488052_11155 {ECO:0000313|EMBL:SEP12991.1};
OS Aquisalimonas asiatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Aquisalimonas.
OX NCBI_TaxID=406100 {ECO:0000313|EMBL:SEP12991.1, ECO:0000313|Proteomes:UP000199657};
RN [1] {ECO:0000313|EMBL:SEP12991.1, ECO:0000313|Proteomes:UP000199657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6291 {ECO:0000313|EMBL:SEP12991.1,
RC ECO:0000313|Proteomes:UP000199657};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC ProRule:PRU01250}.
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DR EMBL; FOEG01000011; SEP12991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8VCE1; -.
DR STRING; 406100.SAMN04488052_11155; -.
DR Proteomes; UP000199657; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 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 InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
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 SMART; SM00994; zf-C4_ClpX; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:SEP12991.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:SEP12991.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SEP12991.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199657};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT DOMAIN 5..59
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ SEQUENCE 393 AA; 41867 MW; EBEBF8B7C9FEA710 CRC64;
MDLSAFHPVE GESSYAICAF CRRGAEQVDE LVAGHDAAMC GDCAAVLHDE VQEQRQAWLR
DRIRNLPTPA RIHGWLDERV VGQEQAKRVL AVQVHNHYKR LALRGMHDAG VVPGKANVLL
SGPTGSGKTH LLRTLAHRLD VPFTVVDATT LTPAGHVGEG VEAIAQGLLR DCDWDPACAA
RGIVYIDEVD KLGGADADGN GVAVQQALLQ LLEGRRIPVT GPRGGRLSMH TRDVLFVAGG
AFTQAVETAA PAPGFVRPSA PGVADDPAQW LLRQGLIPEL VGRFPIHAAL DAVDIPAMRR
LLVEPPDAPL RQMAALVADE GCALEVTARA QDQLASNAIA RATGARGLRG EVERVMLDVL
FELPGRADAR GVVVDVVDGE VRAELQVAQR AAC
//