ID A0A0C2Q9H3_9CYAN Unreviewed; 446 AA.
AC A0A0C2Q9H3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=SD80_28075 {ECO:0000313|EMBL:KIJ80434.1};
OS Scytonema tolypothrichoides VB-61278.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ80434.1};
RN [1] {ECO:0000313|EMBL:KIJ80434.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ80434.1};
RA Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.;
RT "Draft genome sequence of Scytonema tolypothrichoides VB-61278.";
RL Submitted (JAN-2015) 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:KIJ80434.1}.
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DR EMBL; JXCA01000015; KIJ80434.1; -; Genomic_DNA.
DR STRING; 1233231.SD80_28075; -.
DR OrthoDB; 9804062at2; -.
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|HAMAP-Rule:MF_00175};
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:KIJ80434.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW Protease {ECO:0000313|EMBL:KIJ80434.1};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|PROSITE-
KW ProRule:PRU01250}.
FT BINDING 10
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 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 32
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 143..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 446 AA; 49271 MW; 8976A808F71D9C5C CRC64;
MSKYDSHLKC SFCGKSQEQV RKLIAGPGVY ICDECVDLCN EILDEELLDT NGAASSQPAP
KSEPPPKRRA RSSNLSLNQI PKPREIKKYL DEHVIGQDEA KKVLSVAVYN HYKRLSLVQS
KGSGKGLDDA VELQKSNILL IGPTGCGKTL LAQTLAKILD VPFAVADATT LTEAGYVGED
VENILLRLLQ VADLDVEEAQ RGIIYIDEID KIARKSENPS ITRDVSGEGV QQALLKMLEG
TVANVPPQGG RKHPYQDCIQ IDTSNILFVC GGAFVGLEKV VEQRTGKKSI GFVQPGEGQS
KDKRTADTLR YLEPDDLVKF GMIPEFIGRV PMVAVVDPLD EEALMAILTQ PRSALVKQYQ
KLLKMDNVQL EFKPEALRAI AQEAYRRKTG ARALRGIVEE LMLDVMYELP SRKDLTRCTV
TREMVEKRST AELLMHPSTL PKPESA
//