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Database: UniProt
Entry: A0A0J7IYL3_9FLAO
LinkDB: A0A0J7IYL3_9FLAO
Original site: A0A0J7IYL3_9FLAO 
ID   A0A0J7IYL3_9FLAO        Unreviewed;       393 AA.
AC   A0A0J7IYL3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=ATPase AAA {ECO:0000313|EMBL:KMQ71062.1};
GN   ORFNames=ACM44_08945 {ECO:0000313|EMBL:KMQ71062.1};
OS   Chryseobacterium koreense CCUG 49689.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1304281 {ECO:0000313|EMBL:KMQ71062.1, ECO:0000313|Proteomes:UP000035900};
RN   [1] {ECO:0000313|EMBL:KMQ71062.1, ECO:0000313|Proteomes:UP000035900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 49689 {ECO:0000313|EMBL:KMQ71062.1,
RC   ECO:0000313|Proteomes:UP000035900};
RX   PubMed=15545478; DOI=10.1099/ijs.0.02998-0;
RA   Kim M.K., Im W.T., Shin Y.K., Lim J.H., Kim S.H., Lee B.C., Park M.Y.,
RA   Lee K.Y., Lee S.T.;
RT   "Kaistella koreensis gen. nov., sp. nov., a novel member of the
RT   Chryseobacterium-Bergeyella-Riemerella branch.";
RL   Int. J. Syst. Evol. Microbiol. 54:2319-2324(2004).
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:KMQ71062.1}.
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DR   EMBL; LFNG01000011; KMQ71062.1; -; Genomic_DNA.
DR   RefSeq; WP_048499695.1; NZ_LFNG01000011.1.
DR   AlphaFoldDB; A0A0J7IYL3; -.
DR   STRING; 1304281.ACM44_08945; -.
DR   PATRIC; fig|1304281.5.peg.1923; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000035900; 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: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   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};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW   ProRule:PRU01250};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035900};
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   393 AA;  44218 MW;  83A1FEBB2AC44C38 CRC64;
     MNSNQCSFCG RKRNEVKMLV SGNNGFICEN CIEQAHVIVK DSMTKNGFSP ADKIEDLKKP
     KEIKEFLDQY VIGQDQAKKQ LSIAVYNHYK RLLHAKSENK EVEIEKSNII MIGETGTGKT
     LLAKTIAKEL NVPFCIVDAT ILTEAGYVGE DVESILSRLL MVADYDVEKA EKGIVFIDEI
     DKIARKSDNP SITRDVSGEG VQQGLLKLLE GSIVNVPPQG GRKHPDQKYI QVDTKNILFI
     AGGAFDGIKE IIERRLNKQA IGFSSERLNK VEEEDFILSQ INAIDLRKFG LIPELLGRFP
     IVTYLDRLTK ETMIRIMKEP KNSIINQFVE LFKMDGVKLK FTDESIERIV EETIEKGLGA
     RGLRGTTEKV LEDYMFDIAA RKEIVLSGDN VKL
//
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