ID A0A369CBU9_9GAMM Unreviewed; 750 AA.
AC A0A369CBU9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RCX30688.1};
GN ORFNames=DFQ59_104124 {ECO:0000313|EMBL:RCX30688.1};
OS Thioalbus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalbus.
OX NCBI_TaxID=547122 {ECO:0000313|EMBL:RCX30688.1, ECO:0000313|Proteomes:UP000252707};
RN [1] {ECO:0000313|EMBL:RCX30688.1, ECO:0000313|Proteomes:UP000252707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26407 {ECO:0000313|EMBL:RCX30688.1,
RC ECO:0000313|Proteomes:UP000252707};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:RCX30688.1}.
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DR EMBL; QPJY01000004; RCX30688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369CBU9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000252707; 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:0043335; P:protein unfolding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR013461; ClpA.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02639; ClpA; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Hydrolase {ECO:0000313|EMBL:RCX30688.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RCX30688.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252707};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 148..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 83277 MW; FE0E45215A15221F CRC64;
MLSQELEFTL NTAFREAAQK RHEYITVEHL LLALLDNPSA AEVLRACGAN LERLRRELVQ
FVEETTPVFP ASAVEGETQP TLGFQRVLQR AVFHIQSSGK KEVTGANLLV ALFSEQESHA
VYLLREQDIN RLDVLNYVAH GISKVEEEQP LDPESLQDEE QTQAVPGKSP LETYATNLNE
SARRGLIDPL IGRAREVERT IQVLCRRRKN NPLYVGEAGV GKTAIAEGLA RMIVDDQVPE
VLSESTIYAL DLGALLAGTK YRGDFEKRLK AVLHQLENEP GSILFIDEIH TIIGAGAASG
GVMDASNLIK PMLASGQLKC IGATTYQEYR GVFEKDRALA RRFQKIDITE PSVEETVQIL
RGLKSRFEEH HQVKYAPRAL RAAAELADRY INDRHLPDKA IDVIDEVGAR QRLLPPSRRR
RTITVGDVEQ VVASMARIPP KNVSASDKDA LRTLERDLKL AVFGQDTAIE TLGSAIKMSR
AGLGNPDKPI GSFLFAGPTG VGKTEVTRQL ARIMGIELIR FDMSEYMERH TVSRLIGAPP
GYVGYDQGGL LTEAITKHPH AVLLLDEVEK AHPDVFNLLL QVMDHGTLTD NNGRQADFRN
VVLVMTTNAG AELAARPSIG FTSQDHSTDA MEVIRRSFTP EFRNRLDAII QFESLSPVVI
AHVVDKFISE LELQLEEKGV SLEVDESARE WLAEHGYDAQ MGARPMARLI QERIKRPLAE
ELLFGKLAHG GRVNVTARDD ELEFELEAKS
//