GenomeNet

Database: UniProt
Entry: A0A1G7C545_9FLAO
LinkDB: A0A1G7C545_9FLAO
Original site: A0A1G7C545_9FLAO 
ID   A0A1G7C545_9FLAO        Unreviewed;       396 AA.
AC   A0A1G7C545;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:SDE33890.1};
GN   ORFNames=SAMN05421544_10740 {ECO:0000313|EMBL:SDE33890.1};
OS   Riemerella columbipharyngis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Riemerella.
OX   NCBI_TaxID=1071918 {ECO:0000313|EMBL:SDE33890.1, ECO:0000313|Proteomes:UP000198517};
RN   [1] {ECO:0000313|EMBL:SDE33890.1, ECO:0000313|Proteomes:UP000198517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24015 {ECO:0000313|EMBL:SDE33890.1,
RC   ECO:0000313|Proteomes:UP000198517};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01250}.
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; FNAS01000007; SDE33890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7C545; -.
DR   STRING; 1071918.SAMN05421544_10740; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000198517; 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:SDE33890.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:SDE33890.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:SDE33890.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198517};
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   396 AA;  44484 MW;  BD77CA40B0C6D1B4 CRC64;
     MNSNQCSFCG RHRNEVQMLV SGQKGFICEN CIEQAHAIIK DKISHSGGFQ PAESIAELKK
     PREIKKMLDE YVIGQDQAKK QLSIAVYNHY KRLLHAQDES REVEIEKSNI IMIGETGTGK
     TLLAKTIAKE LNVPFCIVDA TILTEAGYVG EDVESILSRL LMVADYDVEK AEKGIVFIDE
     IDKIARKSDN PSITRDVSGE GVQQGLLKLL EGSIVNVPPQ GGRKHPDQKY IQVNTQNILF
     IAGGAFDGIK DIIASRLNKQ AIGFSKDKLK KEEDEEYILH QLNAIDLRKF GLIPELLGRF
     PVITYLDKLT KETMIRIMKE PKNSIVNQFT ELFKMDGIDL KFTDKALEKI VDETMEKGLG
     ARGLRGTTEK VLEHYMFDID ELGGDLSIDE KDIKKL
//
DBGET integrated database retrieval system