ID A0A178HEI4_9LACT Unreviewed; 418 AA. AC A0A178HEI4; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 29-SEP-2021, entry version 25. 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 ORFNames=CYJ29_00900 {ECO:0000313|EMBL:PKZ05002.1}, DBT54_06155 GN {ECO:0000313|EMBL:RAV78866.1}; OS Aerococcus urinae. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus. OX NCBI_TaxID=1376 {ECO:0000313|EMBL:PKZ05002.1, ECO:0000313|Proteomes:UP000234466}; RN [1] {ECO:0000313|EMBL:PKZ05002.1, ECO:0000313|Proteomes:UP000234466} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMB0126 {ECO:0000313|EMBL:PKZ05002.1, RC ECO:0000313|Proteomes:UP000234466}; RA Thomas-White K., Wolfe A.J.; RT "Phylogenetic diversity of female urinary microbiome."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:RAV78866.1, ECO:0000313|Proteomes:UP000251923} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMB7480 {ECO:0000313|EMBL:RAV78866.1, RC ECO:0000313|Proteomes:UP000251923}; RA Hilt E., Gilbert N.M., Thomas-White K., Putonti C., Lewis A.L., Visck K.L., RA Wolfe A.J.; RT "Aerococcus urinae genomes."; RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases. 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:PKZ05002.1}. 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; PKGX01000001; PKZ05002.1; -; Genomic_DNA. DR EMBL; QMHM01000010; RAV78866.1; -; Genomic_DNA. DR RefSeq; WP_064293116.1; NZ_VYWA01000011.1. DR EnsemblBacteria; PKZ05002; PKZ05002; CYJ29_00900. DR EnsemblBacteria; RAV69458; RAV69458; DBT51_00105. DR EnsemblBacteria; RAV78866; RAV78866; DBT54_06155. DR EnsemblBacteria; RAV89825; RAV89825; DBT39_03245. DR Proteomes; UP000234466; Unassembled WGS sequence. DR Proteomes; UP000251923; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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:0006457; P:protein folding; IEA:UniProtKB-UniRule. 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; 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; SSF52540; 1. DR TIGRFAMs; TIGR00382; clpX; 1. DR PROSITE; PS51902; CLPX_ZB; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00175}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175}; KW Hydrolase {ECO:0000313|EMBL:PKZ05002.1}; 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:PKZ05002.1}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}. FT DOMAIN 1..53 FT /note="ClpX-type ZB" FT /evidence="ECO:0000259|PROSITE:PS51902" FT NP_BIND 122..129 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175" FT METAL 12 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175, FT ECO:0000256|PROSITE-ProRule:PRU01250" FT METAL 15 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175, FT ECO:0000256|PROSITE-ProRule:PRU01250" FT METAL 34 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175, FT ECO:0000256|PROSITE-ProRule:PRU01250" FT METAL 37 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175, FT ECO:0000256|PROSITE-ProRule:PRU01250" SQ SEQUENCE 418 AA; 46534 MW; 3B1E3D91AF64C1F2 CRC64; MFNDDNDSNI HCSFCGKSQD QVTKLIAGPD VYICDECVKL CQEIIEDDLN VQSDNQEFIV NPPKPTEIRQ ILDDYVIGQT DAKKALSVAV YNHYKRINSN QIKNQDEDNV ELQKSNILLV GPTGSGKTYL AQTLARILKV PFAIADATSL TEAGYVGEDV ENILLKLLQA ADFDVDKAQQ GIIYIDEIDK IATKAENVSI TRDVSGEGVQ QALLKILEGT VANVPPQGGR KHPHQEFIQI DTTNILFIVG GAFDGIENII KERTGHKVIG FQATKTTKAE KHDLMTQVIP EDLQKYGLIP EFIGRLPIIA SLDELNEEDL ERILTEPKNA LIKQYKQLLA MDNVQLDFTD DSLRAIAQKA IDRKTGARGL RSIIEESMLE VMYDIPSRED VSKVIITEDV VKDHASPELY DQDGQLIA //