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Database: UniProt
Entry: A0A4P7HLS4_9RHOB
LinkDB: A0A4P7HLS4_9RHOB
Original site: A0A4P7HLS4_9RHOB 
ID   A0A4P7HLS4_9RHOB        Unreviewed;       421 AA.
AC   A0A4P7HLS4; A0A4Z1BZC9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:QBX34091.1};
GN   ORFNames=E4191_04755 {ECO:0000313|EMBL:QBX34091.1}, E4L95_11710
GN   {ECO:0000313|EMBL:TGN59386.1};
OS   Paracoccus liaowanqingii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=2560053 {ECO:0000313|EMBL:QBX34091.1, ECO:0000313|Proteomes:UP000296374};
RN   [1] {ECO:0000313|Proteomes:UP000296374, ECO:0000313|Proteomes:UP000297972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2251 {ECO:0000313|Proteomes:UP000296374}, and 3058
RC   {ECO:0000313|EMBL:TGN59386.1, ECO:0000313|Proteomes:UP000297972};
RA   Li J.;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QBX34091.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2251 {ECO:0000313|EMBL:QBX34091.1};
RX   PubMed=31674893;
RA   Li J., Lu S., Jin D., Yang J., Lai X.H., Huang Y., Tian Z., Dong K.,
RA   Zhang S., Lei W., Pu J., Zhang G., Wu X., Huang Y., Ren Z., Wang S., Xu J.;
RT   "Paracoccus liaowanqingii sp. nov., isolated from Tibetan antelope
RT   (Pantholops hodgsonii).";
RL   Int. J. Syst. Evol. Microbiol. 70:744-750(2020).
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}.
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DR   EMBL; CP038439; QBX34091.1; -; Genomic_DNA.
DR   EMBL; SRPG01000104; TGN59386.1; -; Genomic_DNA.
DR   KEGG; plia:E4191_04755; -.
DR   Proteomes; UP000296374; Chromosome.
DR   Proteomes; UP000297972; 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:QBX34091.1};
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:QBX34091.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          3..56
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
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         18
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         40
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         118..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   421 AA;  45853 MW;  4B67BF2C01CD401F CRC64;
     MANQSGNDSK NTLYCSFCGK SQHEVRKLIA GPTVFICDEC VELCMDIIRE ETKSSGLKSG
     DGVPTPREIC GVLDDYVIGQ EHAKRVLSVA VHNHYKRLNH GSKTDIELSK SNILLIGPTG
     CGKTLLAQTL ARILDVPFTM ADATTLTEAG YVGEDVENII LKLLQSSEYN VERAQRGIVY
     IDEVDKITRK SDNPSITRDV SGEGVQQALL KIMEGTVASV PPQGGRKHPQ QEFLQVDTTN
     ILFICGGAFA GLDRIIAQRN AGTAMGFGAA VKEKDDRGVG ELFKELEPED LLKFGLIPEF
     VGRLPVIATL TDLDEEALII ILTKPKNALV KQYQRLFDLE GVQLTFTEDA LTAIAKRAIK
     RKTGARGLRS IMEEILLDTM FELPGLDSVE EVVVNEEAVE STAAKPLLIH ADAKKESASA
     G
//
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