ID I3VU01_THESW Unreviewed; 810 AA.
AC I3VU01;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=ATPase AAA-2 domain protein {ECO:0000313|EMBL:AFK85996.1};
GN OrderedLocusNames=Tsac_0980 {ECO:0000313|EMBL:AFK85996.1};
OS Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK85996.1, ECO:0000313|Proteomes:UP000006178};
RN [1] {ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA Brown S.D., Land M.L., Herring C.D.;
RT "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFK85996.1, ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT Thermoanaerobacterium saccharolyticum during the Degradation of
RT Hemicellulose.";
RL Appl. Environ. Microbiol. 80:5001-5011(2014).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP003184; AFK85996.1; -; Genomic_DNA.
DR RefSeq; WP_014757898.1; NC_017992.1.
DR AlphaFoldDB; I3VU01; -.
DR STRING; 1094508.Tsac_0980; -.
DR KEGG; tsh:Tsac_0980; -.
DR PATRIC; fig|1094508.3.peg.991; -.
DR eggNOG; COG0542; Bacteria.
DR BioCyc; TSAC1094508:GLMA-991-MONOMER; -.
DR Proteomes; UP000006178; Chromosome.
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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 4..145
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 146..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 415..465
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 810 AA; 91315 MW; C3645AFD77668D5F CRC64;
MAMFGRFSEK AQKVLYQAQE EARSLYHNYV GTEHILLGLI KEEDGIASRV LKSLGVTYED
IRSKVESLIG MGNVPGDVVG YTPRAKRVLE LSFAEARRFN TNYIGTEHIL LGLIREGEGV
AVRILMELGV DFNRVREEIV KMVSEEPSGT TNKAQRVKNT NTPNLNQFGR DLTELAREGK
LDPVIGREKE IERVIQILSR RTKNNPCLIG EPGVGKTAIA EGLAEAIESG TIPEILKGKR
VVTLDMASMV AGTKYRGEFE DRLKNVLNEV IKAGNVILFI DELHTIIGAG AAEGAIDASN
ILKPALARGE IQVIGATTID EYRKYIEKDP ALERRFQPIM VEEPSVEETI EILKGLRDKY
EAHHRIKITD EAIEAAAKLS HRYITDRFLP DKAIDLIDEA ASRVRLKTVT APPEIKELED
KLNMLNKDKE EAIRTQEYEK AAKIRDEEQK VKEQLENLKS KWQQNSLVKE KSVGAEEISQ
IVSLWTGIPT QKLAQEESER LLHLEEILHK RVIGQDEAVD AVARAIRRAR VGLKDPKRPI
GSFIFLGPTG VGKTELSKAL AEAMFGDESA IVRIDMSEYM EKFSVSRLIG SPPGYVGYEE
GGELTEKIRR KPYSVILFDE IEKAHPDVFN ILLQILDDGR LTDSKGRTVD FKNTLIIMTS
NVGAQLIKKQ TTLGFMPESN AEKESYEKMK ENILEELKKS FRPEFLNRID DIIVFRQLTQ
DDIRKITDLM IADLNKRLKD NNISLEFTDD AKEELLKEGY DVTYGARPLR RAIQKVVESE
LSELMLKGEI KSGDKILVKL KDGKFDFTKV
//
