ID A0A0Q4EMK4_9FLAO Unreviewed; 395 AA.
AC A0A0Q4EMK4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:KQM50202.1};
GN ORFNames=ASE55_08880 {ECO:0000313|EMBL:KQM50202.1};
OS Chryseobacterium sp. Leaf201.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1735672 {ECO:0000313|EMBL:KQM50202.1, ECO:0000313|Proteomes:UP000051097};
RN [1] {ECO:0000313|EMBL:KQM50202.1, ECO:0000313|Proteomes:UP000051097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf201 {ECO:0000313|EMBL:KQM50202.1,
RC ECO:0000313|Proteomes:UP000051097};
RX PubMed=26633631; DOI=10.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf201 {ECO:0000313|Proteomes:UP000051097};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf201 {ECO:0000313|Proteomes:UP000051097};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQM50202.1}.
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DR EMBL; LMKA01000054; KQM50202.1; -; Genomic_DNA.
DR RefSeq; WP_056216232.1; NZ_LMKA01000054.1.
DR AlphaFoldDB; A0A0Q4EMK4; -.
DR STRING; 1735672.ASE55_08880; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000051097; 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: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 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; 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:0000313|EMBL:KQM50202.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:KQM50202.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KQM50202.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT DOMAIN 1..47
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ SEQUENCE 395 AA; 44293 MW; 8D2920069329C7D6 CRC64;
MNSNQCSFCG RKRNEVQMLI SGQNGFICEN CIEQAHAIVK DSSPESGYAP AENMDELKKP
KEIKKFLDQY VIGQDQAKKQ LSIAVYNHYK RLLHAKEENR EVELEKSNII MIGETGTGKT
LLAKTIAREL NVPFCIVDAT ILTEAGYVGE DVESILSRLL MVADYDVEKA EKGIVFIDEI
DKIARKSDNP SITRDVSGEG VQQGLLKLLE GSIVNVPPQG GRKHPDQKYI QVNTQNILFI
AGGAFDGIKE IIERRMNKQA IGFSSEKINK TGEDEYILTN LNAVDLRSFG LIPELLGRFP
IITYLDKLTK ETMVRIMTEP KNSIVNQFIE LFKMDGTNLV FTDGSIEKIV EETLEKGLGA
RGLRGTTEKV LEDYMFSIGE EKEIILTEDN IFVNK
//