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Entry: A0A0F3IJI9_9GAMM
LinkDB: A0A0F3IJI9_9GAMM
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ID   A0A0F3IJI9_9GAMM        Unreviewed;       426 AA.
AC   A0A0F3IJI9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-SEP-2023, entry version 38.
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=VZ94_16135 {ECO:0000313|EMBL:KJV05714.1};
OS   Methylocucumis oryzae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylocucumis.
OX   NCBI_TaxID=1632867 {ECO:0000313|EMBL:KJV05714.1, ECO:0000313|Proteomes:UP000033684};
RN   [1] {ECO:0000313|Proteomes:UP000033684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sn10-6 {ECO:0000313|Proteomes:UP000033684};
RA   Pandit P.S., Pore S.D., Arora P., Kapse N.G., Dhakephalkar P.K.,
RA   Rahalkar M.C.;
RT   "Draft genome sequence of a novel methanotroph (Sn10-6) isolated from
RT   flooded ricefield rhizosphere in India.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KJV05714.1, ECO:0000313|Proteomes:UP000033684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sn10-6 {ECO:0000313|EMBL:KJV05714.1,
RC   ECO:0000313|Proteomes:UP000033684};
RX   PubMed=26547566; DOI=10.1007/s00248-015-0699-z;
RA   Rahalkar M.C., Pandit P.S., Dhakephalkar P.K., Pore S., Arora P., Kapse N.;
RT   "Genome Characteristics of a Novel Type I Methanotroph (Sn10-6) Isolated
RT   from a Flooded Indian Rice Field.";
RL   Microb. Ecol. 71:519-523(2016).
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:KJV05714.1}.
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DR   EMBL; LAJX01000185; KJV05714.1; -; Genomic_DNA.
DR   RefSeq; WP_045780009.1; NZ_LAJX01000185.1.
DR   AlphaFoldDB; A0A0F3IJI9; -.
DR   PATRIC; fig|1632867.3.peg.2010; -.
DR   OrthoDB; 6378724at2; -.
DR   Proteomes; UP000033684; 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:KJV05714.1};
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:KJV05714.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033684};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          1..50
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   BINDING         9
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         12
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         31
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         34
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         121..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   426 AA;  46592 MW;  EB8F0359F35818FD CRC64;
     MSIKEIKHCS FCGVEQSASI PLIAGAEGYI CGACVALAHQ VVSNWSRKKE LSQMQGELPK
     PSKIKEHLDQ YVIGQHLAKE ILSVAVYNHY KRLKHESGDA GLGEYNKDVE IGKSNILLIG
     PSGTGKTLLA STLAKIVGVP FVVADATTLT QAGYVGEDVE NILVRLLDVA EGNMANAEWG
     IVYLDEVDKI ARSPEQPTGT RDVSGEGVQQ ALLRLVEGSH VKLPNKGRNS TKDGSDLIMD
     TRNILFIAGG SFPGLEKHVE KRLIPTNSAI GFHAAVKQTT VKPSLEDMLN ETQPSDLRKF
     GLIPEFIGRF PVLAPLEPLD VDALIQVLTE PKNALVKQYQ QLFAYEGVNL TFEQEALIEI
     AQKTIERETG ARGLRSIMEQ ILRKTMFEIP SIENVETCVV DADAVKGYSD IKLIKKDDDP
     LRQQAG
//
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