ID R7M9R3_9CLOT Unreviewed; 839 AA.
AC R7M9R3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpA homolog {ECO:0000313|EMBL:CDE97794.1};
GN ORFNames=BN790_00612 {ECO:0000313|EMBL:CDE97794.1};
OS Clostridium sp. CAG:813.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262843 {ECO:0000313|EMBL:CDE97794.1, ECO:0000313|Proteomes:UP000018381};
RN [1] {ECO:0000313|EMBL:CDE97794.1, ECO:0000313|Proteomes:UP000018381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:813 {ECO:0000313|Proteomes:UP000018381};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {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:CDE97794.1}.
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DR EMBL; CBKA010000066; CDE97794.1; -; Genomic_DNA.
DR AlphaFoldDB; R7M9R3; -.
DR Proteomes; UP000018381; 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 Gene3D; 4.10.860.10; UVR domain; 1.
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 InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 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.
DR PROSITE; PS50151; UVR; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:CDE97794.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CDE97794.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 427..462
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 145..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 423..469
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 149..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 92783 MW; 48A8236A44FE614A CRC64;
MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQVLLGLIGE GTGVAAKTLK SMGVNLKDAR
AEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SWDEARQLGH NYIGTEHLLL GLIREGEGVA
ARVLENLGVD LNKVRSNVIK MLGESKPQAT AGAGSSSSSS SSSSSGKTKT PSLDEFGRDL
TLAAQELRLD PVVGREKEIE RVIQILARRT KNNPVLLGEP GVGKTAVAEG LAIRIVNAEV
PDILDGKKVI QLDMGLLVAG TKYRGEFEER LKKIMDEIRQ AGNIILVIDE MHTLIGAGAA
EGAIDAANIL KPALSRGEIQ VIGATTSDEY RKYIEKDSAL ERRFQPVQID EPSIDESIEI
IKGLKPKYEE HHNLVISDEA IVAAVKLSSK YVNDRFLPDK AIDVIDEASS KVRLKASNMC
PEGKELEKQL KTLIKEKEDA IRNQEFETAS QLRDDEADLR DRIREVSAKW REEHDANKPT
VTAENVAEVV AMMTGVPVTK LTEGESERLL KLEDTLHQRV IGQHDAIVAI SKAIRRARVG
LKSPNRPIGS FIFCGPTGVG KTELAKALAE AMFGSEDNMI RVDMSEFMEK HSTAKLIGSP
PGYVGYDDGG HLSELVRKKP YSVVLFDEIE KAHPDVFNIM LQILDDGRLT DSKGRHISFK
NTVIIMTSNV GASMITNTSK LGFTTAEDES KSKYEKLKDT VSEEMKKAFR PEFLNRIDET
IVFAHLSKEE IRQIVDLMLK DLFKRLAEKE LNIDVSDEVK DYLAENGYSE AYGARPLRRL
IQRKMEDSLA EEILSGKYGK GDTIKVSLVD GKITFDKASK AKRAKKEKEA EPTEETATN
//
