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Database: UniProt
Entry: A0A1Q2CFK8_9ACTN
LinkDB: A0A1Q2CFK8_9ACTN
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ID   A0A1Q2CFK8_9ACTN        Unreviewed;       425 AA.
AC   A0A1Q2CFK8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   ORFNames=RPIT_08800 {ECO:0000313|EMBL:AQP44877.1}, SAMN05428934_10770
GN   {ECO:0000313|EMBL:SDY97731.1};
OS   Tessaracoccus flavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=1610493 {ECO:0000313|EMBL:AQP44877.1, ECO:0000313|Proteomes:UP000188324};
RN   [1] {ECO:0000313|EMBL:AQP44877.1, ECO:0000313|Proteomes:UP000188324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RP1T {ECO:0000313|EMBL:AQP44877.1,
RC   ECO:0000313|Proteomes:UP000188324};
RX   PubMed=26869509; DOI=10.1099/ijsem.0.000958;
RA   Kumari R., Singh P., Schumann P., Lal R.;
RT   "Tessaracoccus flavus sp. nov., isolated from the drainage system of a
RT   lindane-producing factory.";
RL   Int. J. Syst. Evol. Microbiol. 66:1862-1868(2016).
RN   [2] {ECO:0000313|EMBL:SDY97731.1, ECO:0000313|Proteomes:UP000199635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RP1 {ECO:0000313|EMBL:SDY97731.1,
RC   ECO:0000313|Proteomes:UP000199635};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AQP44877.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RP1T {ECO:0000313|EMBL:AQP44877.1};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; CP019605; AQP44877.1; -; Genomic_DNA.
DR   EMBL; FNPU01000007; SDY97731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2CFK8; -.
DR   STRING; 1610493.RPIT_08800; -.
DR   KEGG; tfl:RPIT_08800; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000188324; Chromosome.
DR   Proteomes; UP000199635; 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; IPR001496; SOCS_box.
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.
DR   PROSITE; PS50225; SOCS; 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:AQP44877.1};
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:AQP44877.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188324};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          1..54
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   DOMAIN          41..78
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   BINDING         13
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         16
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         35
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         38
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         124..131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   425 AA;  46338 MW;  1EA077AD50A38ADE CRC64;
     MARIGESGDL FKCNFCGKSQ KQVKKLIAGP GVYICDECIA LCNEIIEEEF PETTDTGLVE
     ELPKPREIRD FLDSYVIGQD TAKKTLSVAV YNHYKRIQAQ QSHGRRAEND DVEVGKSNIL
     LIGPTGCGKT YLAQTLAKML NVPFAMADAT ALTEAGYVGE DVENILLKLI QAADFDIAKA
     ETGIIYIDEI DKVARKSENP SITRDVSGEG VQQALLKILE GTVASVPPQG GRKHPHQDFL
     QIDTTKILFI VGGAFAGLEE IINARVGKRP LGFNNSAEAR EPSAEPFAQV RPEDLHKFGL
     IPEFIGRLPM LTSVSPLDRD ALVRILVEPK NALTRQFQKL FELDGVQLEF TDDAVGAIAD
     LALERGTGAR GLRAILESLL LETMFDVPSD EDVAQVVVTA EAVRGEALPT LIPRAQLASR
     RDLSA
//
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