GenomeNet

Database: UniProt
Entry: A0A1V4IL35_9CLOT
LinkDB: A0A1V4IL35_9CLOT
Original site: A0A1V4IL35_9CLOT 
ID   A0A1V4IL35_9CLOT        Unreviewed;       429 AA.
AC   A0A1V4IL35;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN   Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175,
GN   ECO:0000313|EMBL:OPJ60455.1};
GN   ORFNames=CLCHR_29410 {ECO:0000313|EMBL:OPJ60455.1}, D2A34_08815
GN   {ECO:0000313|EMBL:RII35298.1}, GKZ28_00525
GN   {ECO:0000313|EMBL:MVX62184.1};
OS   Clostridium chromiireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=225345 {ECO:0000313|EMBL:OPJ60455.1, ECO:0000313|Proteomes:UP000191056};
RN   [1] {ECO:0000313|EMBL:OPJ60455.1, ECO:0000313|Proteomes:UP000191056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23318 {ECO:0000313|EMBL:OPJ60455.1,
RC   ECO:0000313|Proteomes:UP000191056};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium chromiireducens DSM 23318.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RII35298.1, ECO:0000313|Proteomes:UP000265930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C1 {ECO:0000313|EMBL:RII35298.1,
RC   ECO:0000313|Proteomes:UP000265930};
RA   Xing M., Wei Y., Ang E.L., Zhao H., Zhang Y.;
RT   "Genome of Clostridium chromiireducens C1, DSM12136.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MVX62184.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NM79_F5 {ECO:0000313|EMBL:MVX62184.1};
RA   Navarre W., Wong E.;
RT   "Microbes associate with the intestines of laboratory mice.";
RL   Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC       directs the protease to specific substrates. Can perform chaperone
CC       functions in the absence of ClpP. {ECO:0000256|HAMAP-Rule:MF_00175}.
CC   -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC       that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC       into a disk-like structure with a central cavity, resembling the
CC       structure of eukaryotic proteasomes. {ECO:0000256|HAMAP-Rule:MF_00175}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|HAMAP-
CC       Rule:MF_00175, ECO:0000256|PROSITE-ProRule:PRU01250}.
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:OPJ60455.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; WSRQ01000001; MVX62184.1; -; Genomic_DNA.
DR   EMBL; MZGT01000039; OPJ60455.1; -; Genomic_DNA.
DR   EMBL; QXDJ01000002; RII35298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4IL35; -.
DR   STRING; 225345.CLCHR_29410; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000191056; Unassembled WGS sequence.
DR   Proteomes; UP000265930; Unassembled WGS sequence.
DR   Proteomes; UP000656077; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0000256|HAMAP-
KW   Rule:MF_00175};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW   Hydrolase {ECO:0000313|EMBL:OPJ60455.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00175}; Protease {ECO:0000313|EMBL:OPJ60455.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191056};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          1..53
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         116..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   429 AA;  47829 MW;  2974005E212F2A9E CRC64;
     MAKYDEKKQL KCSFCGKTQE QVKRLIAGPG VYICDECIDL CSEIIADEFQ ETVDFDPKSV
     PKPNEIKEYL DSYVIGQERA KKSLAVAVYN HYKRINTNKE DIDVELSKSN ILLLGPTGSG
     KTLLAQTLAR FLNVPFAIAD ATTLTEAGYV GEDVENILLK LIQNADYDVE KAERGIIYID
     EIDKIARKSE NPSITRDVSG EGVQQALLKI LEGTVASVPP QGGRKHPHQE FIQINTSNIL
     FICGGAFDGV DKIIENRTRK SSMGFGAEIQ AKNEKDVGSL LKEIMPADLL KFGLIPEFVG
     RLPILVTLES LDRDALIQIL TKPKNALVKQ YKKLFELDDV KLDFDEKSLN AIADEAISRQ
     TGARGLRAII EDIMNEVMYE IPSDNRITKV TITEDAIKDK KEPKIERVEE GKIRPTLVKA
     RAKKDIESA
//
DBGET integrated database retrieval system