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Database: UniProt
Entry: E8R055_ISOPI
LinkDB: E8R055_ISOPI
Original site: E8R055_ISOPI 
ID   E8R055_ISOPI            Unreviewed;       478 AA.
AC   E8R055;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 78.
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   OrderedLocusNames=Isop_0580 {ECO:0000313|EMBL:ADV61173.1};
OS   Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Isosphaera.
OX   NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV61173.1, ECO:0000313|Proteomes:UP000008631};
RN   [1] {ECO:0000313|EMBL:ADV61173.1, ECO:0000313|Proteomes:UP000008631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43644 / DSM 9630 / IS1B
RC   {ECO:0000313|Proteomes:UP000008631};
RX   PubMed=21475588; DOI=10.4056/sigs.1533840;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Isosphaera pallida type strain (IS1B).";
RL   Stand. Genomic Sci. 4:63-71(2011).
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; CP002353; ADV61173.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8R055; -.
DR   STRING; 575540.Isop_0580; -.
DR   KEGG; ipa:Isop_0580; -.
DR   eggNOG; COG1219; Bacteria.
DR   HOGENOM; CLU_014218_8_2_0; -.
DR   InParanoid; E8R055; -.
DR   OMA; HYKRVQA; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000008631; Chromosome.
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:ADV61173.1};
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:ADV61173.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008631};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          24..78
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36
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         39
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         59
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         62
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         143..150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   478 AA;  52030 MW;  6D7806ADD1D7ED21 CRC64;
     MASGRDNSGG HAGSKRNSGG GSPPSGPGGG KRNAICSFCR KSYREVGPLV EGPADVYICG
     ECIELCQSIL EKDRRSRGGR SLFGEIPNPR EIKAQLDQYV IGQDRAKKVL SVAVHNHYKR
     LVHDEEPETD VELDKSNILL IGPTGSGKTL LARTLARVLN VPFAIGDATT LTEAGYVGED
     VENILLKLLH AANFDLEAAQ RGIVYIDEID KIGKTSHNVS ITRDVSGEGV QQALLKMLEG
     TVANVPPQGG RKHPEQQYIQ MDTTNILFIC GGTFVGLDNI IARRIGRKTI GFGGAMGDSD
     SAREKNLADL LNQVTSDDVL EFGLIPEFIG RLPVICPLMP LDVEALVQIL TEPRNALVKQ
     YQRLFEMEGA KLQFDSEALR EIAILAKERD TGARGLRSII EDTMLDIMFE LPERPDKTEK
     IFLVTPAVVR REVSLFDSTL PRVVEESAHP PAEGDPEATT QADPQTSAQD PSSRKESA
//
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