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Database: UniProt
Entry: A0A2C6MCI2_9FIRM
LinkDB: A0A2C6MCI2_9FIRM
Original site: A0A2C6MCI2_9FIRM 
ID   A0A2C6MCI2_9FIRM        Unreviewed;       364 AA.
AC   A0A2C6MCI2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-SEP-2023, entry version 21.
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=P378_19375 {ECO:0000313|EMBL:PHJ36936.1};
OS   Desulforamulus profundi.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1383067 {ECO:0000313|EMBL:PHJ36936.1, ECO:0000313|Proteomes:UP000222564};
RN   [1] {ECO:0000313|EMBL:PHJ36936.1, ECO:0000313|Proteomes:UP000222564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bs107 {ECO:0000313|EMBL:PHJ36936.1,
RC   ECO:0000313|Proteomes:UP000222564};
RA   Aullo T., Berlendis S., Lascourreges J.-F., Dessort D., Saint-Laurent S.,
RA   Schraauwers B., Mas J., Magot M., Ranchou-Peyruse A.;
RT   "Biodegradation of hydrocarbons in the deep terrestrial subsurface :
RT   characterization of a microbial consortium composed of two Desulfotomaculum
RT   species originating from a deep geological formation.";
RL   Submitted (SEP-2013) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00175}.
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:PHJ36936.1}.
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DR   EMBL; AWQQ01000133; PHJ36936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C6MCI2; -.
DR   Proteomes; UP000222564; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein 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; 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   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   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW   Hydrolase {ECO:0000313|EMBL:PHJ36936.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW   Protease {ECO:0000313|EMBL:PHJ36936.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222564};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          53..273
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          257..352
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   364 AA;  40090 MW;  DD139BBC4571E728 CRC64;
     MDMGDLPKPK EIKAILDQYV IGQENAKRQL AVAVYNHYKR INLGGKVEDV ELSKSNIVML
     GPTGCGKTLL AQTLARLLNV PFAIADATSL TEAGYVGEDV ENILLKLIQA ADYDVEKAEK
     GIVYIDEIDK IARKSENPSI TRDVSGEGVQ QALLKILEGT VASVPPQGGR KHPHQEFIQL
     DTTNILFICG GAFDGIEKII QNRTGKKQLG FGAEIQTKRE QKIGEILANI LPEDLLKFGL
     IPEFVGRLPV IVTLDALDEE ALIRILTEPK NALAKQYEKL FELDGVSLEI QPDALGEVAK
     EALKRNTGAR GLRAIMEEAM LNIMYDIPSR KDISKVIITK EAILKKGEPL LITMENKKKK
     EESA
//
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