ID A0A6I5BB73_9ACTN Unreviewed; 432 AA. AC A0A6I5BB73; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 14-DEC-2022, entry version 9. DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175}; GN Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175, GN ECO:0000313|EMBL:MYQ53186.1}; GN ORFNames=GTW41_18540 {ECO:0000313|EMBL:MYQ53186.1}; OS Streptomyces sp. SID4941. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=2690283 {ECO:0000313|EMBL:MYQ53186.1, ECO:0000313|Proteomes:UP000450528}; RN [1] {ECO:0000313|EMBL:MYQ53186.1, ECO:0000313|Proteomes:UP000450528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SID4941 {ECO:0000313|EMBL:MYQ53186.1, RC ECO:0000313|Proteomes:UP000450528}; RX PubMed=30705269; DOI=.1038/s41467-019-08438-0; RA Chevrette M.G., Carlson C.M., Ortega H.E., Thomas C., Ananiev G.E., RA Barns K.J., Book A.J., Cagnazzo J., Carlos C., Flanigan W., Grubbs K.J., RA Horn H.A., Hoffmann F.M., Klassen J.L., Knack J.J., Lewin G.R., RA McDonald B.R., Muller L., Melo W.G.P., Pinto-Tomas A.A., Schmitz A., RA Wendt-Pienkowski E., Wildman S., Zhao M., Zhang F., Bugni T.S., Andes D.R., RA Pupo M.T., Currie C.R.; RT "The antimicrobial potential of Streptomyces from insect microbiomes."; RL Nat. Commun. 10:516-516(2019). CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It CC directs the protease to specific substrates. Can perform chaperone CC functions in the absence of ClpP. {ECO:0000256|HAMAP-Rule:MF_00175}. CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled CC into a disk-like structure with a central cavity, resembling the CC structure of eukaryotic proteasomes. {ECO:0000256|HAMAP-Rule:MF_00175}. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|HAMAP- CC Rule:MF_00175, ECO:0000256|PROSITE-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:MYQ53186.1}. 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; WWJA01000192; MYQ53186.1; -; Genomic_DNA. DR RefSeq; WP_028439717.1; NZ_WWJA01000192.1. DR AlphaFoldDB; A0A6I5BB73; -. DR Proteomes; UP000450528; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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 Gene3D; 3.40.50.300; -; 1. DR Gene3D; 6.20.220.10; -; 1. DR HAMAP; MF_00175; ClpX; 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; IPR046425; ClpX_bact. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010603; Znf_CppX_C4. DR InterPro; IPR038366; Znf_CppX_C4_sf. 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR00382; clpX; 1. DR PROSITE; PS51902; CLPX_ZB; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000313|EMBL:MYQ53186.1}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175}; KW Hydrolase {ECO:0000313|EMBL:MYQ53186.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00175}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175}; KW Protease {ECO:0000313|EMBL:MYQ53186.1}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}. FT DOMAIN 1..54 FT /note="ClpX-type ZB" FT /evidence="ECO:0000259|PROSITE:PS51902" FT REGION 412..432 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175, FT ECO:0000256|PROSITE-ProRule:PRU01250" FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175, FT ECO:0000256|PROSITE-ProRule:PRU01250" FT BINDING 35 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175, FT ECO:0000256|PROSITE-ProRule:PRU01250" FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175, FT ECO:0000256|PROSITE-ProRule:PRU01250" FT BINDING 123..130 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175" SQ SEQUENCE 432 AA; 47346 MW; A49E8B2AF1E40A3E CRC64; MARIGDGGDL LKCSFCGKSQ KQVKKLIAGP GVYICDECID LCNEIIEEEL AESSEVRWEE LPKPREIYEF LEGYVVGQEP AKKALSVAVY NHYKRVQAGE NGGGANRDDA IELAKSNILL LGPTGSGKTL LAQTLARMLN VPFAIADATA LTEAGYVGED VENILLKLIQ AADYDVKKAE TGIIYIDEID KVARKSENPS ITRDVSGEGV QQALLKILEG TTASVPPQGG RKHPHQEFIQ IDTTNVLFIV GGAFSGLEKI IESRAGAKGI GFGATIRSKR EIQASDQFQE VMPEDLVKFG MIPEFIGRLP VLTSVHNLDR EALLQILVEP RNALVKQYQR LFELDGVELD FEREALEAIA DQAILRQTGA RGLRAIMEEV LQSVMYEVPS RKDVARVVIT PDVVRDNVNP TLVPREPRTI GTNDGGRHEK SA //