ID K7VVS7_9NOST Unreviewed; 447 AA.
AC K7VVS7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
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:AFW92902.1};
GN ORFNames=ANA_C10090 {ECO:0000313|EMBL:AFW92902.1};
OS Anabaena sp. 90.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW92902.1, ECO:0000313|Proteomes:UP000010101};
RN [1] {ECO:0000313|EMBL:AFW92902.1, ECO:0000313|Proteomes:UP000010101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90 {ECO:0000313|EMBL:AFW92902.1};
RX PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT cyanobacterium Anabaena sp. strain 90.";
RL BMC Genomics 13:613-613(2012).
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}.
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DR EMBL; CP003284; AFW92902.1; -; Genomic_DNA.
DR RefSeq; WP_015078066.1; NC_019427.1.
DR AlphaFoldDB; K7VVS7; -.
DR STRING; 46234.ANA_C10090; -.
DR KEGG; anb:ANA_C10090; -.
DR PATRIC; fig|46234.3.peg.101; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_3; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000010101; Chromosome chANA01.
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:AFW92902.1};
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:AFW92902.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010101};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 1..51
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 51..77
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: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 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 447 AA; 49423 MW; 2268F5BAC4186C9A CRC64;
MSKYDSHLKC SFCGKSQEQV RKLIAGPGVY ICDECVDLCN EILDEELLDT NTAAASQPTQ
KSEPAEKRRT RSSNLSFNQI PKPREIKNYL DEHVIGQDEA KKVLSVAVYN HYKRLAILQA
KGSAKVEADD AIELQKSNIL LIGPTGCGKT LLAQTLAKIL DVPFAVADAT TLTEAGYVGE
DVENILLRLL QVADLDVEEA QRGIIYIDEI DKIARKSENP SITRDVSGEG VQQALLKMLE
GTVANVPPQG GRKHPYQDCI QIDTSNILFV CGGAFVGLEK VVDQRVGKKS IGFVQPGDVQ
TKEKRAADTL RHLQPDDLVK FGMIPEFIGR IPMVAVVDPL DEDALMAILT EPRSALVKQY
QKLLNMDNVQ LDFKPDALRA IAQEAYRRKT GARALRGIVE ELMLDVMYEL PSRKDVTRCT
ITKEMVEKRS TAELIVHPSS LPKPESA
//
