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Database: UniProt
Entry: A0A5C6F0F3_9BACT
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ID   A0A5C6F0F3_9BACT        Unreviewed;       430 AA.
AC   A0A5C6F0F3;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
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:TWU54525.1};
GN   ORFNames=Poly51_32440 {ECO:0000313|EMBL:TWU54525.1};
OS   Rubripirellula tenax.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rubripirellula.
OX   NCBI_TaxID=2528015 {ECO:0000313|EMBL:TWU54525.1, ECO:0000313|Proteomes:UP000318288};
RN   [1] {ECO:0000313|EMBL:TWU54525.1, ECO:0000313|Proteomes:UP000318288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Poly51 {ECO:0000313|EMBL:TWU54525.1,
RC   ECO:0000313|Proteomes:UP000318288};
RA   Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA   Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA   Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA   Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA   Labrenz M., Spormann A.M., Op Den Camp H., Overmann J., Amann R.,
RA   Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA   Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT   "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT   characterization uncovers novel biology.";
RL   Submitted (FEB-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:TWU54525.1}.
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DR   EMBL; SJPW01000004; TWU54525.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C6F0F3; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000318288; 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:TWU54525.1};
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:TWU54525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000318288};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          14..68
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   BINDING         26
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         29
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         49
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         52
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         134..141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   430 AA;  47356 MW;  1143D12DE8AF39CF CRC64;
     MPSKDNPPTT TTSRRGTSTN KKNAFCSFCR KSYRDVGPLV EGPGDVYICS ECIELCQSIL
     DQEQRRRGPS KSLFNDIPTP RSIVEHLDQY VIGQGSAKRV LAVAVHNHYK RLTSEWEGGS
     EVEIEKSNIL LAGPTGSGKT LLARSLARML NVPFAIGDAT TLTEAGYVGE DVENLLLKLL
     HAADFDVEAA QRGILYIDEV DKIGKTSANV SITRDVSGEG VQQSLLKMLE GTVANVPPQG
     GRKHPEQQYI QMDTSNILFI VGGTFVGIED IIRKRLGHKT LGFGGGDSKR NEQTESELLA
     QVQTEDILQF GLIPELVGRL PVVSYLQPLD EEGLVNVMTQ PKNSLIKQYE ALFQMENCEL
     KFTEEALHYV ARKALNKGVG ARGLRGILEE VMLDIMYDLP EQPEGTLYTI DENVVSGKNK
     LFQMPTTKSA
//
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