ID S0FH67_RUMCE Unreviewed; 817 AA.
AC S0FH67;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=ATPases with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:EMS71010.1};
GN ORFNames=CTER_3251 {ECO:0000313|EMBL:EMS71010.1};
OS Ruminiclostridium cellobioparum subsp. termitidis CT1112.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=1195236 {ECO:0000313|EMBL:EMS71010.1, ECO:0000313|Proteomes:UP000014155};
RN [1] {ECO:0000313|EMBL:EMS71010.1, ECO:0000313|Proteomes:UP000014155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT1112 {ECO:0000313|EMBL:EMS71010.1,
RC ECO:0000313|Proteomes:UP000014155};
RX PubMed=23704187;
RA Lal S., Ramachandran U., Zhang X., Munir R., Sparling R., Levin D.B.;
RT "Draft Genome Sequence of the Cellulolytic, Mesophilic, Anaerobic Bacterium
RT Clostridium termitidis Strain CT1112 (DSM 5398).";
RL Genome Announc. 1:E00281-13(2013).
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:EMS71010.1}.
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DR EMBL; AORV01000044; EMS71010.1; -; Genomic_DNA.
DR RefSeq; WP_004627268.1; NZ_AORV01000044.1.
DR AlphaFoldDB; S0FH67; -.
DR STRING; 1195236.CTER_3251; -.
DR PATRIC; fig|1195236.3.peg.3474; -.
DR eggNOG; COG0542; Bacteria.
DR Proteomes; UP000014155; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000014155};
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 419..454
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 144..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 415..465
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 144..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 91266 MW; AC5745E9396E39C4 CRC64;
MYQRFTEKAE RAISFSQQSA VELGHNYVGT EHILLGLVKE GTGVAARVLQ AQGITEEKIS
REIDELIGRG ETAGETPVGF TPRTKRVLEL AFKEARRMGQ GYIGTEHLLL GIMKEGESVA
VRIMMDLGVD PQKLLNELVK ILNEETPGSN GSPKNSSSNS STPTLNQFGR DLTDMARDGK
IDPVIGRDKE IERVIQILSR RTKNNPCLIG EPGVGKTAIA EGLAQKIVEG NIPEILSDKR
VVTLDLSSMV AGAKYRGEFE DRLKKAMEEI RKAGNVILFI DELHTIVGAG AAEGAIDASN
ILKPSLARGE IQVIGATTLN EYRKHIEKDA ALERRFQPIT VGEPSKEEAV EILKGVRDKY
EAHHRVKITD DALEASVKLS DRYITDRFLP DKAIDLVDEA ASRIRLKTFT APPDIKDMEE
RVDKLSKEKE DSIRCQEFEK AARIRDEEQK LKNELEKVKD QWHQRNQTKT DTVTADDIAD
IVASWTGIPV KKLAEEESER LLKMEDTLHN RVIGQDEAVK SISRAIRRGR VGLKDPKRPV
GSFIFLGPTG VGKTELCKAL AEAMFGDEKS MIRVDMSEFM EKHSVSKLVG SPPGYVGYDE
GGQLTEKVRR RPYSVLLFDE IEKAHPDIFN ILLQILEDGR LTDSQGRVVD FRNTIIIMTS
NVGARTITEP KRLGFSAVKD ESAKNYEDMK SNVMGELKKM FRPEFLNRID DIIVFHPLTE
ENIREIVKLM TDVLVKRLKA NEIDLEISEE LLLHLAKKGY DPIFGARPLR RAIQSMVEDK
LAEEMLEGKV KAGDSIKVGM DGDNIVVTRK TGNLVKA
//
