ID A0A132P9J9_ENTFC Unreviewed; 416 AA.
AC A0A132P9J9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 51.
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:BDP57462.1};
GN ORFNames=AWT83_11235 {ECO:0000313|EMBL:KWX19015.1}, B1P95_09970
GN {ECO:0000313|EMBL:OOL82290.1}, DPX30_08510
GN {ECO:0000313|EMBL:RAQ24348.1}, EfmJHP36_19410
GN {ECO:0000313|EMBL:BDP57462.1}, GBM44_08210
GN {ECO:0000313|EMBL:KAB7617931.1}, GBM73_01380
GN {ECO:0000313|EMBL:KAB7576042.1}, IQN16_07970
GN {ECO:0000313|EMBL:UOC30735.1}, KT858_002000
GN {ECO:0000313|EMBL:HBH6537733.1};
OS Enterococcus faecium (Streptococcus faecium).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1352 {ECO:0000313|EMBL:KWX19015.1, ECO:0000313|Proteomes:UP000070452};
RN [1] {ECO:0000313|EMBL:KWX19015.1, ECO:0000313|Proteomes:UP000070452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D344RRF x C68 {ECO:0000313|EMBL:KWX19015.1,
RC ECO:0000313|Proteomes:UP000070452};
RA Garcia-Solache M.A., Lebreton F., Mclaughlin R.E., Whiteaker J.D.,
RA Gilmore M.S., Rice L.B.;
RT "Molecular Mechanisms for transfer of large genomic segments between
RT Enterococcus faecium strains.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OOL82290.1, ECO:0000313|Proteomes:UP000191171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIM1759 {ECO:0000313|EMBL:OOL82290.1,
RC ECO:0000313|Proteomes:UP000191171};
RA Marchi A.P., Martins R.C., Marie S.K., Levin A.S., Costa S.F.;
RT "Clonality and virulence of isolates of VRE in Hematopoietic Stem Cell
RT Transplanted (HSCT) patients.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:HBH6537733.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=V2279 {ECO:0000313|EMBL:HBH6537733.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [4] {ECO:0000313|EMBL:RAQ24348.1, ECO:0000313|Proteomes:UP000249226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A20 {ECO:0000313|EMBL:RAQ24348.1,
RC ECO:0000313|Proteomes:UP000249226};
RA Zhou X., Chlebowicz M.A., Bathoorn E., Rosema S., Couto N., Lokate M.,
RA Arends J.P., Friedrich A.W., Rossen J.W.;
RT "Elucidating vancomycin-resistant Enterococcus faecium outbreaks: the role
RT of clonal spread and movement of mobile genetic elements.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Proteomes:UP000446843, ECO:0000313|Proteomes:UP000469871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VRECG10 {ECO:0000313|EMBL:KAB7617931.1,
RC ECO:0000313|Proteomes:UP000446843}, and VRECG27
RC {ECO:0000313|EMBL:KAB7576042.1, ECO:0000313|Proteomes:UP000469871};
RA Chilambi G.S., Nordstrom H.R., Evans D.R., Ferrolino J., Hayden R.T.,
RA Maron G.M., Vo A.N., Gilmore M.S., Wolf J., Rosch J.W., Van Tyne D.;
RT "Evolutionary dynamics of vancomycin-resistant Enterococcus faecium during
RT gastrointestinal tract colonization and bloodstream infection in
RT immunocompromised pediatric patients.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:HBH6537733.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=V2279 {ECO:0000313|EMBL:HBH6537733.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:UOC30735.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BMT-1-1-10 {ECO:0000313|EMBL:UOC30735.1};
RX PubMed=35134550;
RA Both A., Kruse F., Mirwald N., Franke G., Christner M., Huang J.,
RA Hansen J.L., Kroger N., Berneking L., Lellek H., Aepfelbacher M., Rohde H.;
RT "Population dynamics in colonizing vancomycin-resistant Enterococcus
RT faecium isolated from immunosuppressed patients.";
RL J Glob Antimicrob Resist 28:267-273(2022).
RN [8] {ECO:0000313|EMBL:BDP57462.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JHP36 {ECO:0000313|EMBL:BDP57462.1};
RA Hashimoto Y., Suzuki M., Tomita H.;
RT "Analysis of enterococcal linear plasmids.";
RL Submitted (AUG-2022) 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}.
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DR EMBL; AP026586; BDP57462.1; -; Genomic_DNA.
DR EMBL; DAERWN010000043; HBH6537733.1; -; Genomic_DNA.
DR EMBL; WEFP01000001; KAB7576042.1; -; Genomic_DNA.
DR EMBL; WEGG01000001; KAB7617931.1; -; Genomic_DNA.
DR EMBL; LRHK01000001; KWX19015.1; -; Genomic_DNA.
DR EMBL; MVGJ01000054; OOL82290.1; -; Genomic_DNA.
DR EMBL; QLYM01000001; RAQ24348.1; -; Genomic_DNA.
DR EMBL; CP063555; UOC30735.1; -; Genomic_DNA.
DR RefSeq; WP_002288492.1; NZ_WMGZ01000012.1.
DR PATRIC; fig|1352.1358.peg.1555; -.
DR OMA; HYKRVQA; -.
DR Proteomes; UP000070452; Unassembled WGS sequence.
DR Proteomes; UP000191171; Unassembled WGS sequence.
DR Proteomes; UP000249226; Unassembled WGS sequence.
DR Proteomes; UP000446843; Unassembled WGS sequence.
DR Proteomes; UP000469871; Unassembled WGS sequence.
DR Proteomes; UP000831402; Chromosome.
DR Proteomes; UP000885039; Unassembled WGS sequence.
DR Proteomes; UP001061325; Chromosome.
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 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 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 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:0000256|HAMAP-
KW Rule:MF_00175};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW Hydrolase {ECO:0000313|EMBL:KWX19015.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00175}; Protease {ECO:0000313|EMBL:KWX19015.1};
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 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 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 416 AA; 46226 MW; FAF751F14DE5EF50 CRC64;
MYDNPSSNET VRCSFCGKTQ EEVKKIVAGP GVYICNECID LCKEIIDEEF YEEAVREFTE
VPKPLEILEV LNNYVIGQDR AKRSLAVAVY NHYKRVNQQA QENTDDVELQ KSNICLIGPT
GSGKTFLAQT LAKTLNVPFA IADATSLTEA GYVGEDVENI LLKLLQSADY NVELAEKGII
YIDEIDKIAR KSENVSITRD VSGEGVQQAL LKILEGTVAS VPPQGGRKHP HQEFIQIDTT
NILFIVGGAF DGIETIVKNR MGEKTIGFGT QNQKLSEDES VMQHIIPEDL LKFGLIPEFI
GRLPVMAALE KLTTDDLVRI LTEPKNALVK QYQKLLSLDN TELEFEPEAL RAIAKKAIER
NTGARGLRSI IEEIMMDVMF DIPSNENIEK VIITKEAAEL SGEPTVIYKD SEKKAG
//