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Database: UniProt
Entry: A0A0E3ZUT1_9BACT
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Original site: A0A0E3ZUT1_9BACT 
ID   A0A0E3ZUT1_9BACT        Unreviewed;       410 AA.
AC   A0A0E3ZUT1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=ATPase AAA {ECO:0000313|EMBL:AKD54713.1};
GN   ORFNames=SD10_07115 {ECO:0000313|EMBL:AKD54713.1};
OS   Spirosoma radiotolerans.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD54713.1, ECO:0000313|Proteomes:UP000033054};
RN   [1] {ECO:0000313|EMBL:AKD54713.1, ECO:0000313|Proteomes:UP000033054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5A {ECO:0000313|EMBL:AKD54713.1,
RC   ECO:0000313|Proteomes:UP000033054};
RX   PubMed=24748440; DOI=10.1007/s00284-014-0584-x;
RA   Lee J.J., Srinivasan S., Lim S., Joe M., Im S., Bae S.I., Park K.R.,
RA   Han J.H., Park S.H., Joo B.M., Park S.J., Kim M.K.;
RT   "Spirosoma radiotolerans sp. nov., a gamma-radiation-resistant bacterium
RT   isolated from gamma ray-irradiated soil.";
RL   Curr. Microbiol. 69:286-291(2014).
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01250}.
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DR   EMBL; CP010429; AKD54713.1; -; Genomic_DNA.
DR   RefSeq; WP_046376316.1; NZ_CP010429.1.
DR   AlphaFoldDB; A0A0E3ZUT1; -.
DR   STRING; 1379870.SD10_07115; -.
DR   KEGG; srd:SD10_07115; -.
DR   PATRIC; fig|1379870.5.peg.1546; -.
DR   HOGENOM; CLU_014218_8_2_10; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000033054; Chromosome.
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:UP000033054};
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   410 AA;  45818 MW;  04806D4E43EE8A45 CRC64;
     MPQISCSFCG RRKNEVMMLL SGIDAHICNY CIEQGHQVVL EEMRPKKSEP AEVNIKLIKP
     VDMKRHLDQF VVGQDDAKKA ITVAVYNHYK RLMQPKTNDD VTIEKSNIIM VGETGTGKTY
     LARSIAKILE VPFCIADATV ITEAGYVGED VETILTRLLQ AADYNVEAAE RGIVYIDEID
     KIARKSDNPS ITRDVSGEGV QQALLKLLEG SVVNVPPQGG RKHPDQRLIA LNTEHILFIC
     GGAFDGIERH ITKRINTRPI GFSGDRRLND TFERGHLMRY ISALDLKSFG LIPELIGRLP
     VLTHLEPLDR NALMQILTEP KNAITKQYDK LFKMEGITLH WDPSALNYIV DQALQYGLGA
     RGLRSICESI ITDAMFEMPS QTGVTELTVS LEYAREKFGK SGTHQLRSVA
//
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