ID A0A098TH87_9CYAN Unreviewed; 170 AA.
AC A0A098TH87;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=ClpX-type ZB domain-containing protein {ECO:0000259|PROSITE:PS51902};
DE Flags: Fragment;
GN ORFNames=DO97_14830 {ECO:0000313|EMBL:KGF71337.1};
OS Neosynechococcus sphagnicola sy1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC Neosynechococcaceae; Neosynechococcus.
OX NCBI_TaxID=1497020 {ECO:0000313|EMBL:KGF71337.1, ECO:0000313|Proteomes:UP000030170};
RN [1] {ECO:0000313|EMBL:KGF71337.1, ECO:0000313|Proteomes:UP000030170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAUP A 1101 {ECO:0000313|EMBL:KGF71337.1,
RC ECO:0000313|Proteomes:UP000030170};
RA Dvorak P., Casamatta D., Hasler P., Poulickova A., Ondrej V., Sanges R.;
RT "Evolution of Synechococcus.";
RL Mol. Ecol. 0:0-0(2014).
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC 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:KGF71337.1}.
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DR EMBL; JJML01000113; KGF71337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098TH87; -.
DR STRING; 1497020.DO97_14830; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000030170; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0006457; P:protein folding; IEA:UniProtKB-UniRule.
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 InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
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; PF00004; AAA; 1.
DR Pfam; PF06689; zf-C4_ClpX; 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};
KW Chaperone {ECO:0000256|PROSITE-ProRule:PRU01250};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01250};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030170};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01250}.
FT DOMAIN 4..57
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT NON_TER 170
FT /evidence="ECO:0000313|EMBL:KGF71337.1"
SQ SEQUENCE 170 AA; 18820 MW; 44A67EA098696660 CRC64;
MAEKKRLLPA KKPLYCSFCG KSQHEVKKLI AGPSVFICDE CIDLCNEIIR DELPAGDLAR
EGRSDLPTPV EIKTNLDNYV IGQEVAKRTL AVAVYNHYKR LRHKDKAHKD DVELSKSNIL
LIGPTGSGKT LLAQTLARML DVPFVMADAT TLTEAGYVGE DVENIVQKLL
//
