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Database: UniProt
Entry: A0A0D4C2J4_9MICC
LinkDB: A0A0D4C2J4_9MICC
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ID   A0A0D4C2J4_9MICC        Unreviewed;       427 AA.
AC   A0A0D4C2J4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=UM93_05745 {ECO:0000313|EMBL:AJT42912.1};
OS   Psychromicrobium lacuslunae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Psychromicrobium.
OX   NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT42912.1, ECO:0000313|Proteomes:UP000061839};
RN   [1] {ECO:0000313|EMBL:AJT42912.1, ECO:0000313|Proteomes:UP000061839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT42912.1,
RC   ECO:0000313|Proteomes:UP000061839};
RX   PubMed=25908143;
RA   Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K.,
RA   Gulati A.;
RT   "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter sp.
RT   Strain IHBB 11108 Using PacBio Single-Molecule Real-Time Sequencing
RT   Technology.";
RL   Genome Announc. 3:0-0(2015).
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; CP011005; AJT42912.1; -; Genomic_DNA.
DR   RefSeq; WP_045076958.1; NZ_CP011005.1.
DR   AlphaFoldDB; A0A0D4C2J4; -.
DR   STRING; 1618207.UM93_05745; -.
DR   KEGG; ari:UM93_05745; -.
DR   PATRIC; fig|1618207.4.peg.1168; -.
DR   HOGENOM; CLU_014218_8_2_11; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000061839; 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:AJT42912.1};
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:AJT42912.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061839};
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         126..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   427 AA;  46290 MW;  467FF200E61882BC CRC64;
     MARMGESTDL LKCSFCGKSQ KQVRKLIAGP GVYICDECIE LCNEIIEEEL AEVADLGSFE
     LPKPKEIFNF LQEYVIGQEP AKRSLSVAVY NHYKRIQAGS KGQALADGSH HDDVEIAKSN
     ILLIGPTGCG KTYLAQTLAR RLNVPFAVAD ATALTEAGYV GEDVENILLK LIQAADYDVK
     KAEQGIIYID EIDKISRKSE NPSITRDVSG EGVQQALLKI LEGTVASVPP QGGRKHPHQE
     FIQIDTTNVL FIVAGAFAGL EEIIGARAGK KGIGFGAPLG ALSGEEASYG DVMPEDLLKF
     GLIPEFIGRL PVITTVSHLD RDALIQILTE PKNALIKQYQ KMFHLDGVEL SFEDEALDAI
     ADQALERGTG ARGLRAILEE VLLPVMFELP SRDDIASAVV TAESVKESGQ LTLIPHDVVA
     KRRNKSA
//
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