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Database: UniProt
Entry: F4LRW3_TEPAE
LinkDB: F4LRW3_TEPAE
Original site: F4LRW3_TEPAE 
ID   F4LRW3_TEPAE            Unreviewed;       813 AA.
AC   F4LRW3; L0S5R4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Class III stress response-related ATPase, AAA+ superfamily {ECO:0000313|EMBL:CCP27183.1};
GN   Name=clpC {ECO:0000313|EMBL:CCP27183.1};
GN   OrderedLocusNames=TEPIRE1_2348 {ECO:0000313|EMBL:CCP27183.1};
OS   Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Tepidanaerobacteraceae; Tepidanaerobacter.
OX   NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP27183.1, ECO:0000313|Proteomes:UP000010802};
RN   [1] {ECO:0000313|Proteomes:UP000010802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX   PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA   Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT   "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT   Tepidanaerobacter acetatoxydans strain Re1.";
RL   Genome Announc. 1:E00213-E00213(2013).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; HF563609; CCP27183.1; -; Genomic_DNA.
DR   RefSeq; WP_013779221.1; NC_019954.2.
DR   AlphaFoldDB; F4LRW3; -.
DR   STRING; 1209989.TepRe1_2180; -.
DR   KEGG; tae:TepiRe1_2348; -.
DR   KEGG; tep:TepRe1_2180; -.
DR   PATRIC; fig|1209989.3.peg.2698; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000010802; 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   Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          414..449
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          410..456
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   813 AA;  91485 MW;  E822121568268127 CRC64;
     MNGRFTERAQ KVIAYAQEEA RRLNHNVVGT EHLLLGLLRE GEGVAARALI NLGVDADKVR
     SQVEMMIGVG PFPIQGPIGY TPRAKRVMEL AIDESRRLGH NYVGTEHILL GLIREGEGVA
     AQVLANLGVS LDKAREEVLN LLVDSKAQGS YKKSANTPTL NQFGRDLTEL AAEGKLDPVV
     GREKEIERVI QVLTRRTKNN PCLIGEPGVG KTAVVEGLAQ QIIEQNVPEI LKDKRVVSLD
     MASLVAGTKF RGEFEERLKK VMTEIKQAGN VILFIDEMHT IIGAGAAEGA IDASNILKPA
     LARGEIQTIG ATTIDEYRKY VEKDPALERR FQPIMVEEPT VEETIQILKG LRDRYEAHHR
     VKISDEAIEA AAKLSYRYIT DRFLPDKAID LIDEAASRVR LKTLTAPPEL REMEDKLEAI
     RKEKDAAIRA QEFEKAASLR DKEQEVKAEV EKLKELWQKD YKFENSTVKE EDIAHIVAIW
     TGIPVKRLTE EESERLLKLE EVLHNRVIGQ DEAVKAVAKA IRRAYAGLKD PARPIGSFIF
     LGPTGVGKTE LARALADAMF GDEDAMIRLD MSEYMEKFAV SRIVGAPPGY VGYEEGGELT
     EKVRRRPYSV ILFDEIEKAH PDVFNILLQI LEDGRLTDAK GRTVDFRNTI LIMTSNVGAN
     LIQKPKVLGF APVQEEEKSY AEMKDMVLNE LKRTFKPEFL NRIDEIIVFH PLSEEHIREI
     VTLMIDEVNR RLTEKQISIE VTDKAKDVLA KEGYDPMYGA RPLRRVIQKR IEDRLSEEML
     KGSITDGDVV LVDVDEDEKE FTFKKKELTT TKF
//
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