CLPX_SYNS3
ID CLPX_SYNS3 Reviewed; 451 AA.
AC Q0IE20;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; OrderedLocusNames=sync_0064;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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:0000255|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:0000255|HAMAP-Rule:MF_00175}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC Rule:MF_00175}.
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DR EMBL; CP000435; ABI47536.1; -; Genomic_DNA.
DR RefSeq; WP_011618053.1; NC_008319.1.
DR AlphaFoldDB; Q0IE20; -.
DR SMR; Q0IE20; -.
DR STRING; 64471.sync_0064; -.
DR EnsemblBacteria; ABI47536; ABI47536; sync_0064.
DR KEGG; syg:sync_0064; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_3; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 718259at2; -.
DR Proteomes; UP000001961; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.20.220.10; -; 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 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; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..451
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_1000024692"
FT DOMAIN 1..51
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT REGION 50..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ SEQUENCE 451 AA; 49221 MW; 3192BD0D94366DCE CRC64;
MAKFDAHLKC SFCGKSQEQV RKLIAGPGVY ICDECIDLCN EILDEELIDA QGNPRHGAEP
SKKTAAGGTR KTSKPAPTLA TIPKPQEIKG FLDEQVVGQE AAKKVMSVAV YNHYKRLAWQ
GDGQGEAAQT ATRLHKSNIL LIGPTGCGKT LLAQTLAEML DVPFAVADAT TLTEAGYVGE
DVENILLRLL QKADMDVEQA QRGIIYIDEI DKIARKSENP SITRDVSGEG VQQALLKMLE
GTVANVPPQG GRKHPYQDCI QIDTSQILFI CGGAFVGLDD VVQKRMGRNA IGFVPNDGRG
RNRATRDIQA AQVLRHLEPD DLVKYGLIPE FIGRMPVSAV LEPLDEHALE SILTEPRDAL
VKQFSTLLSM DNVQLDFEAQ AVEAIAKEAH RRKTGARALR GIVEELMLDL MYELPSDQNV
TAFTITKAMV EEHTGGKVLP LPGTKQHKES A