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Database: UniProt
Entry: X5J9G2_9BACT
LinkDB: X5J9G2_9BACT
Original site: X5J9G2_9BACT 
ID   X5J9G2_9BACT            Unreviewed;       421 AA.
AC   X5J9G2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   13-SEP-2023, entry version 43.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:CDG49694.1};
DE            EC=3.4.21.92 {ECO:0000313|EMBL:CDG49694.1};
GN   Name=clpX {ECO:0000313|EMBL:CDG49694.1};
GN   ORFNames=CHV_a0381 {ECO:0000313|EMBL:CDG49694.1};
OS   Cardinium endosymbiont cBtQ1 of Bemisia tabaci.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Candidatus Cardinium.
OX   NCBI_TaxID=1354314 {ECO:0000313|EMBL:CDG49694.1, ECO:0000313|Proteomes:UP000024482};
RN   [1] {ECO:0000313|EMBL:CDG49694.1, ECO:0000313|Proteomes:UP000024482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cBtQ1 {ECO:0000313|Proteomes:UP000024482};
RX   DOI=10.1093/gbe/evu077;
RA   Santos-Garcia D., Rollat-Farnier P.A., Beitia F., Zchori-Fein E., Vavre F.,
RA   Mouton L., Moya A., Latorre A., Silva F.J.;
RT   "The genome of Cardinium cBtQ1 provides insights into genome reduction,
RT   symbiont motility and its settlement in Bemisia tabaci.";
RL   Genome Biol. Evol. Evol.0:0-0(2014).
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:CDG49694.1}.
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DR   EMBL; CBQZ010000001; CDG49694.1; -; Genomic_DNA.
DR   RefSeq; WP_034576758.1; NZ_CBQZ010000001.1.
DR   AlphaFoldDB; X5J9G2; -.
DR   STRING; 1354314.CHV_a0381; -.
DR   eggNOG; COG1219; Bacteria.
DR   Proteomes; UP000024482; 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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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:CDG49694.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:CDG49694.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:CDG49694.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024482};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT   DOMAIN          1..46
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   BINDING         5
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ   SEQUENCE   421 AA;  46598 MW;  C9C77F846A20FA3D CRC64;
     MKTHCSFCKK ASEIVSMMVT GPEGRICDQC VTQAAQIIQL QKEDNIINDI KPVNLLRPQE
     IKAYLDEYVI GQEEAKKALS IAVYNHYKRL SHPANIEDDV VIEKSNILLV GETGTGKTYL
     VRTLAQMLEV PFCIVDATVL TEAGYVGEDV ESIISRLLHA ANYEVTAAER GIVYVDEIDK
     IARKGDNPSI TRDVSGEGVQ QSLLKLLEGS IVNAPPHGGR KHPDQKLTAV NTEKILFICG
     GAFDGIARTI SNRINFNSIG FEFCAKRTPK VDDKDILKYV SSSDIKGYGL IPELVGRLPI
     VRGFEPLTKS DLRRILTEPK NALVKQYTKL FAIDGIALTF TEETLDLIAE QAISLKLGAR
     GLRSICESIM SEVMYTAPSL KDQQKLVIDK AYALEQLGRT QIELLKQIEK NSQASELKKM
     A
//
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