ID E4TZS1_SULKY Unreviewed; 403 AA.
AC E4TZS1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:ADR34178.1};
DE EC=3.4.21.92 {ECO:0000313|EMBL:ADR34178.1};
GN OrderedLocusNames=Sulku_1516 {ECO:0000313|EMBL:ADR34178.1};
OS Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 /
OS YK-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfuricurvum.
OX NCBI_TaxID=709032 {ECO:0000313|EMBL:ADR34178.1, ECO:0000313|Proteomes:UP000008721};
RN [1] {ECO:0000313|EMBL:ADR34178.1, ECO:0000313|Proteomes:UP000008721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1
RC {ECO:0000313|Proteomes:UP000008721};
RX PubMed=22675602; DOI=10.4056/sigs.2456004;
RA Han C., Kotsyurbenko O., Chertkov O., Held B., Lapidus A., Nolan M.,
RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Brambilla E.M., Rohde M., Spring S.,
RA Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of the sulfur compounds oxidizing
RT chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T)).";
RL Stand. Genomic Sci. 6:94-103(2012).
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC ProRule:PRU01250}.
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DR EMBL; CP002355; ADR34178.1; -; Genomic_DNA.
DR RefSeq; WP_013460375.1; NC_014762.1.
DR AlphaFoldDB; E4TZS1; -.
DR STRING; 709032.Sulku_1516; -.
DR KEGG; sku:Sulku_1516; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_7; -.
DR OMA; KSNMLMI; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000008721; 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: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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ADR34178.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:ADR34178.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:ADR34178.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008721};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT DOMAIN 1..48
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ SEQUENCE 403 AA; 44340 MW; 0EBFCF23D79A338E CRC64;
MQPEKTCSFC GRKQSEVKKM FSSETTHICN ECVTTCSSIL QKEVRYEQRS AMQQQLPTPE
KIVEFLNKYI IGQEDAKKVL AVALYNHYKR IENPVYNNVE LEKSNIMLVG PTGSGKTLLA
KSLSKIMQVP FAVADATALT EAGYVGEDVE SILSRLLAAA NYDIDLAQRG IIYIDEVDKI
ARKGESSTMG RDVSGEGVQQ GLLKILEGAE VYVPIKGSRK NSTTETVLFN TSHVLFVCGG
AFVGLVPDTH TKKTNKVGFS KSASADAKPK KIDAKALVHY GMIPEFIGRI PVVAQLGELT
KDQMIQILQE PDNALIKQFQ ALFDMDGIEL NFEDKALEAV AQKAIDRGVG ARGLRGIIEE
AMLPLQFSCP SKKNLQSVTV TEAVIENPDN EPIYVYKEEH AEA
//