ID J1ADS5_9FLAO Unreviewed; 410 AA.
AC J1ADS5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
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:EJG00254.1};
GN ORFNames=FF52_16514 {ECO:0000313|EMBL:EJG00254.1};
OS Flavobacterium sp. F52.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1202532 {ECO:0000313|EMBL:EJG00254.1, ECO:0000313|Proteomes:UP000002690};
RN [1] {ECO:0000313|EMBL:EJG00254.1, ECO:0000313|Proteomes:UP000002690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F52 {ECO:0000313|EMBL:EJG00254.1,
RC ECO:0000313|Proteomes:UP000002690};
RX PubMed=22965088; DOI=10.1128/JB.01249-12;
RA Kolton M., Green S.J., Harel Y.M., Sela N., Elad Y., Cytryn E.;
RT "Draft Genome Sequence of Flavobacterium sp. Strain F52, Isolated from the
RT Rhizosphere of Bell Pepper (Capsicum annuum L. cv. Maccabi).";
RL J. Bacteriol. 194:5462-5463(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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00175}.
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:EJG00254.1}.
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; AKZQ01000032; EJG00254.1; -; Genomic_DNA.
DR RefSeq; WP_008467306.1; NZ_AKZQ01000032.1.
DR AlphaFoldDB; J1ADS5; -.
DR PATRIC; fig|1202532.3.peg.3383; -.
DR eggNOG; COG1219; Bacteria.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000002690; Unassembled WGS sequence.
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; IPR025662; Sigma_54_int_dom_ATP-bd_1.
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.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 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:EJG00254.1};
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:EJG00254.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 1..49
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 8
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 11
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 30
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 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
SQ SEQUENCE 410 AA; 45498 MW; 42BCA0488AD1AA40 CRC64;
MAKVVLECSF CGRKKPETNL LIAGINAHIC DKCIEQAHGI VLEELKSSGS AKLVGDLILK
KPKEIRAFLD QYVIGQDQTK KVMSVAVYNH YKRLMQQQLD DEVEIEKSNI IMVGQTGTGK
TLVAKTIAKM LDVPLAIVDA TVLTEAGYVG EDVESILTRL LQAADYDVAK AERGIVFIDE
IDKIARKSDN PSITRDVSGE GVQQALLKLL EGTVVNVPPK GGRKHPDQKF VEVNTQNILF
IAGGAFDGVE RIISKRLNRQ AVGYSTSKNT DNIDKDNLLQ YIIPKDIKDF GLIPEIIGRL
PVLTHMDPLD KATLRAILTQ PKNALIKQYQ KLFLMDDVEF TITDEALDFI VDKALEYKLG
ARGLRSLCEA ILTDAMYELP TSDDISLTID KEYAEHTLSK NLLKRMEIAS
//