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Database: UniProt
Entry: A0A2G1XFY3_STRCJ
LinkDB: A0A2G1XFY3_STRCJ
Original site: A0A2G1XFY3_STRCJ 
ID   A0A2G1XFY3_STRCJ        Unreviewed;       428 AA.
AC   A0A2G1XFY3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
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:GHC50793.1};
GN   ORFNames=BLA24_20810 {ECO:0000313|EMBL:PHQ50049.1}, CYQ11_09970
GN   {ECO:0000313|EMBL:PPT13172.1}, GCM10010507_28300
GN   {ECO:0000313|EMBL:GHC50793.1};
OS   Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces cinnamoneus group.
OX   NCBI_TaxID=53446 {ECO:0000313|EMBL:PHQ50049.1, ECO:0000313|Proteomes:UP000222531};
RN   [1] {ECO:0000313|EMBL:PHQ50049.1, ECO:0000313|Proteomes:UP000222531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21532 {ECO:0000313|EMBL:PHQ50049.1,
RC   ECO:0000313|Proteomes:UP000222531};
RX   PubMed=29053243;
RA   Patteson J., Cai W., Johnson R.A., Santa Maria K., Li B.;
RT   "Identification of the Biosynthetic Pathway for the Antibiotic
RT   Bicyclomycin.";
RL   Biochemistry 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:PPT13172.1, ECO:0000313|Proteomes:UP000239771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41675 {ECO:0000313|EMBL:PPT13172.1,
RC   ECO:0000313|Proteomes:UP000239771};
RA   Vior N.M., Lacret R., Chandra G., Dorai-Raj S., Trick M., Truman A.W.;
RT   "Discovery and biosynthesis of the antibiotic bicyclomycin in distant
RT   bacterial classes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:GHC50793.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4633 {ECO:0000313|EMBL:GHC50793.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [4] {ECO:0000313|EMBL:GHC50793.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4633 {ECO:0000313|EMBL:GHC50793.1};
RA   Sun Q., Ohkuma M.;
RL   Submitted (SEP-2020) 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:PHQ50049.1}.
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DR   EMBL; BMVB01000008; GHC50793.1; -; Genomic_DNA.
DR   EMBL; NHZO01000151; PHQ50049.1; -; Genomic_DNA.
DR   EMBL; PKFQ01000001; PPT13172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G1XFY3; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000222531; Unassembled WGS sequence.
DR   Proteomes; UP000239771; Unassembled WGS sequence.
DR   Proteomes; UP000646244; 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   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:PHQ50049.1};
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:PHQ50049.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222531};
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          409..428
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         122..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   428 AA;  46877 MW;  E8232D0B5BC5E11E CRC64;
     MARIGDGGDL LKCSFCGKSQ KQVKKLIAGP GVYICDECID LCNEIIEEEL AETSEVRWEE
     LPKPREIYEF LEGYVVGQEA AKKALSVAVY NHYKRVQAGE NGGHNRDDGI ELAKSNILLL
     GPTGSGKTLL AQTLARMLNV PFAIADATAL TEAGYVGEDV ENILLKLIQA ADYDVKKAET
     GIIYIDEIDK VARKSENPSI TRDVSGEGVQ QALLKILEGT TASVPPQGGR KHPHQEFIQI
     DTTNVLFIVG GAFSGLEKII ESRAGAKGIG FGATIRSKRE IEASDQFQEV MPEDLVKFGM
     IPEFIGRLPV ITSVHNLDRE ALLQILVEPR NALVKQYQRL FELDGVELDF DRPALEAIAD
     QAILRGTGAR GLRAIMEEVL MSVMYEVPSR KDVARVVITA DVVQSNVNPT LVPRTRGNEP
     GERHEKSA
//
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