ID Q8GDW8_HELMO Unreviewed; 420 AA.
AC Q8GDW8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 13-SEP-2023, entry version 109.
DE SubName: Full=ATP-dependent clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:AAN87458.1};
DE SubName: Full=ATP-dependent protease ATP-binding subunit ClpX {ECO:0000313|EMBL:MTV48673.1};
DE Flags: Fragment;
GN Name=clpX {ECO:0000313|EMBL:MTV48673.1};
GN ORFNames=GJ688_06735 {ECO:0000313|EMBL:MTV48673.1};
OS Heliobacterium mobile (Heliobacillus mobilis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliobacterium.
OX NCBI_TaxID=28064 {ECO:0000313|EMBL:AAN87458.1};
RN [1] {ECO:0000313|EMBL:AAN87458.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12446909; DOI=10.1126/science.1075558;
RA Raymond J., Zhaxybayeva O., Gogarten J.P., Gerdes S.Y., Blankenship R.E.;
RT "Whole-genome analysis of photosynthetic prokaryotes.";
RL Science 298:1616-1620(2002).
RN [2] {ECO:0000313|EMBL:AAN87458.1}
RP NUCLEOTIDE SEQUENCE.
RA Liolios K.G., Chu L., Ostrovskaya O., Mendybaeva N., Koukharenko V.,
RA Gerdes S., Kyrpides N., Overbeek R.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MTV48673.1, ECO:0000313|Proteomes:UP000430670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6151 {ECO:0000313|EMBL:MTV48673.1,
RC ECO:0000313|Proteomes:UP000430670};
RA Kyndt J.A., Meyer T.E.;
RT "Whole-genome sequence of a the green, strictly anaerobic photosynthetic
RT bacterium Heliobacillus mobilis DSM 6151.";
RL Submitted (NOV-2019) 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; AY142854; AAN87458.1; -; Genomic_DNA.
DR EMBL; WNKU01000005; MTV48673.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GDW8; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000430670; 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: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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19497; RecA-like_ClpX; 1.
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 HAMAP; MF_00175; ClpX; 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; IPR046425; ClpX_bact.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
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 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 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:AAN87458.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:AAN87458.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:AAN87458.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000430670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT DOMAIN 2..55
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT NON_TER 420
FT /evidence="ECO:0000313|EMBL:AAN87458.1"
SQ SEQUENCE 420 AA; 46611 MW; 939D3374832E61AF CRC64;
MYKGFGDDKG QLKCSFCGKL QDQVKKLVAG PGVYICDECI ELCNEIIEEE LQDENTFDLG
DVPKPKEIRE ILDQYVIGQD QAKKALSVAV YNHYKRINLG SKIDDIELQK SNIVMLGPTG
SGKTLLAQTL ARILNVPFAI ADATSLTEAG YVGEDVENIL LKLIQAADYD VEKAEKGIVY
IDEIDKIARK SENPSITRDV SGEGVQQALL KILEGTVASV PPQGGRKHPH QEFIQLDTTN
ILFICGGAFD GIDKLIMNRV GKKAMGFNAD IKGKQDKNIG EVLRDILPGD LLKFGLIPEF
VGRLPVIVTL DALDEDALVR ILTEPKNALI KQYQKFFELD QVNLEFQDEA LRAIAHEAIK
RNTGARGLRA IIEEVMLDVM FDIPSRNDVT KCMVTKEVIL KQKEPVLVTA DRKKKKEESA
//