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Database: UniProt
Entry: A0A080LUU0_9PROT
LinkDB: A0A080LUU0_9PROT
Original site: A0A080LUU0_9PROT 
ID   A0A080LUU0_9PROT        Unreviewed;       333 AA.
AC   A0A080LUU0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:KFB71420.1};
GN   Name=clpX_2 {ECO:0000313|EMBL:KFB71420.1};
GN   ORFNames=AW09_003424 {ECO:0000313|EMBL:KFB71420.1};
OS   Candidatus Accumulibacter phosphatis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=327160 {ECO:0000313|EMBL:KFB71420.1, ECO:0000313|Proteomes:UP000020077};
RN   [1] {ECO:0000313|EMBL:KFB71420.1, ECO:0000313|Proteomes:UP000020077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA-91 {ECO:0000313|Proteomes:UP000020077};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KFB71420.1}.
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DR   EMBL; JDVG02000544; KFB71420.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A080LUU0; -.
DR   Proteomes; UP000020077; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR000641; CbxX/CfxQ.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
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   PRINTS; PR00819; CBXCFQXSUPER.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KFB71420.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:KFB71420.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:KFB71420.1}.
FT   DOMAIN          51..224
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          239..324
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          88..115
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   333 AA;  37125 MW;  D6D508D5E734ADCD CRC64;
     MLTRETTPSA IVRYLDQYVI GQDEAKKILA VAVYSHYRKI ATFAKDKGSF AKSNVLLVGP
     SGTGKTLLCD TLSRMLDVPF VTADATSLAQ TKYVNEEIEA ALQRLLEKAD GNVENAQHGI
     IFIDEIDKLK ATPAESRATS GESVQHALLK IMEGSPVKLK NNQYIDTSNV LFICGGAFVG
     LEKIMSKTHG FGFIATSTDD NQNILDRLNQ RVKPTDLFEF GLIPEFTGRL PVIANLHPLS
     KAMLVSIMSV PKNSIYRQYI EIFRGEGVEL SIGQRVFEQI AEIAIEYKTG ARSLRGIFEE
     LITPILYVVP DKPEICKVEI RSLFEDARFF RRK
//
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