CLPX_SYNE7
ID CLPX_SYNE7 Reviewed; 449 AA.
AC O34126; Q31K63;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
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};
GN OrderedLocusNames=Synpcc7942_2526;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12101312; DOI=10.1099/00221287-148-7-2255;
RA Schelin J., Lindmark F., Clarke A.K.;
RT "The clpP multigene family for the ATP-dependent Clp protease in the
RT cyanobacterium Synechococcus.";
RL Microbiology 148:2255-2265(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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: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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U92039; AAB68678.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58556.1; -; Genomic_DNA.
DR RefSeq; WP_011243893.1; NC_007604.1.
DR AlphaFoldDB; O34126; -.
DR SMR; O34126; -.
DR STRING; 1140.Synpcc7942_2526; -.
DR PRIDE; O34126; -.
DR EnsemblBacteria; ABB58556; ABB58556; Synpcc7942_2526.
DR KEGG; syf:Synpcc7942_2526; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_3; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 718259at2; -.
DR BioCyc; MetaCyc:SYNPCC7942_2526-MON; -.
DR BioCyc; SYNEL:SYNPCC7942_2526-MON; -.
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; Zinc.
FT CHAIN 1..449
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_0000160441"
FT DOMAIN 1..51
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT REGION 49..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Polar residues"
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 146..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
FT CONFLICT 128
FT /note="E -> EF (in Ref. 1; AAB68678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49836 MW; 88A9D9C5121C7310 CRC64;
MSRYDSHLKC SFCGKSQEQV RKLIAGPGVY ICDECVDLCN EILDEELFDG NANPAPPPGS
PKPATAATTS HQGPRKPKRS LTLSQIPKPH DIKRYLDHHV IGQNEAKKML SVAVYNHYKR
LAYQQSAEEA GETIEIQKSN ILLIGPTGCG KTLLAQTLAK LLDVPFAVAD ATTLTEAGYV
GEDVENILLR LLQVADLDIE EAQRGIIYID EIDKIARKSE NPSITRDVSG EGVQQALLKM
LEGTIANVPP QGGRKHPYQD CIQIDTRNIL FICGGAFVGL EKLVDRRLGK KSIGFVHPEE
SKTKEQRAAA ILRHMEPEDL VQFGLIPEFI GRMPVTAVLD PLDETALTEI LTEPRDALVK
QYQKLMHMDS VELEFRQDAI EAIAREAFRR KTGARALRGI VEEIMLEVMY ELPSRQDVTH
CTITREMVEK RSSADVLLLP SSLPTPESA
