ID A0A1H7B757_9DEIO Unreviewed; 739 AA.
AC A0A1H7B757;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SEJ72694.1};
GN ORFNames=SAMN04488058_11614 {ECO:0000313|EMBL:SEJ72694.1};
OS Deinococcus reticulitermitis.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=856736 {ECO:0000313|EMBL:SEJ72694.1, ECO:0000313|Proteomes:UP000199223};
RN [1] {ECO:0000313|Proteomes:UP000199223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10218 {ECO:0000313|Proteomes:UP000199223};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FNZA01000016; SEJ72694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7B757; -.
DR STRING; 856736.SAMN04488058_11614; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199223; 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 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; 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 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; 2.
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:SEJ72694.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEJ72694.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..65
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 144..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 78644 MW; 9264DF8D08585024 CRC64;
MISERLQATL QRAVDLAREA GHEYVTQEHL LLALLDDLDA QEVLLAVGVN IPRLQGTLED
ALAGFEGVED AEPDFTLGVH RVVQGAVLQL HASGKAHEQA DGGRVLAELL EEEDSPARAA
VEAQGVTRLD VLSYLSHGAA RVAGRSREKR GAGADGGALP EAGPDEADPL GAYASDLTAQ
ARAGEFDPVI GREAELTRMV HVLARRTKNN PVLVGEPGVG KTALAEGLAQ RVVDGQAPGF
LKGASVYALN LGALLAGTRY RGDFEQRLGA VLAALEGQNA VLFIDELHTI VGAGATEGGS
VDAANLLKPA LARGGLRVLG ATTPAELRHL EKDRALWRRF QTVEVPEPSE EDALAILRGL
EGRYAEHHGV SFTPDALEAA VRLSVRHLRD RFLPDKAIDV LDEAGAARSS AGRGGVLGVP
DIEATVARMA RVPVGAVRAE EVTSLATLAD DLRRRVYGQD AAVDAVAGAV KLARAGLRDP
QKPQGMFLFA GPTGVGKTEL ARALADRLGI HLARFDMSEY QEAHTVARLI GAPPGYVGFD
QGGLLTDAVA KNPHAVLLLD EIEKAHPDVY NIFLQLMDHG TLTDHAGKKV DGRGLILIFT
TNAGAADASR PALGFSREGR SGEEAEAVKR TFSPEFRNRL DAVIHFRPLS RGVMGSVVDK
FIRRLAAQLA ERNVQLEVSG EARELLAELG YDPLLGARPL ARVIEHQLGR PLAEAVLFGR
LQGGGSVQVR REGRELTFD
//