ID A0A178HEI4_9LACT Unreviewed; 418 AA. AC A0A178HEI4; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00645734}; GN Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175}; GN ORFNames=A1D21_07660 {ECO:0000313|EMBL:OAM70820.1}; OS Aerococcus urinae. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Aerococcus. OX NCBI_TaxID=1376 {ECO:0000313|EMBL:OAM70820.1, ECO:0000313|Proteomes:UP000078342}; RN [1] {ECO:0000313|EMBL:OAM70820.1, ECO:0000313|Proteomes:UP000078342} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AU3 {ECO:0000313|EMBL:OAM70820.1, RC ECO:0000313|Proteomes:UP000078342}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. CC It directs the protease to specific substrates. Can perform CC chaperone functions in the absence of ClpP. {ECO:0000256|HAMAP- CC Rule:MF_00175, ECO:0000256|SAAS:SAAS00645739}. CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric CC ring that, in the presence of ATP, binds to fourteen ClpP subunits CC assembled into a disk-like structure with a central cavity, CC resembling the structure of eukaryotic proteasomes. CC {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00645732}. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. CC {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00701777}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAM70820.1}. 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; LUKP01000030; OAM70820.1; -; Genomic_DNA. DR RefSeq; WP_064293116.1; NZ_LUKP01000030.1. DR EnsemblBacteria; OAM70820; OAM70820; A1D21_07660. DR Proteomes; UP000078342; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. 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 PANTHER; PTHR11262; PTHR11262; 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; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00382; clpX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00175, KW ECO:0000256|SAAS:SAAS00701780, ECO:0000313|EMBL:OAM70820.1}; KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00175, KW ECO:0000256|SAAS:SAAS00645733}; KW Complete proteome {ECO:0000313|Proteomes:UP000078342}; KW Hydrolase {ECO:0000313|EMBL:OAM70820.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175, KW ECO:0000256|SAAS:SAAS00645729}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175, KW ECO:0000256|SAAS:SAAS00701776}; KW Protease {ECO:0000313|EMBL:OAM70820.1}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00645735}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00175, KW ECO:0000256|SAAS:SAAS00645738}. FT DOMAIN 9 48 zf-C4_ClpX. {ECO:0000259|SMART:SM00994}. FT DOMAIN 113 263 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 315 409 ClpB_D2-small. {ECO:0000259|SMART: FT SM01086}. FT ZN_FING 12 37 C4-type. {ECO:0000256|HAMAP-Rule: FT MF_00175}. FT NP_BIND 122 129 ATP. {ECO:0000256|HAMAP-Rule:MF_00175}. 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 //