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Database: UniProt
Entry: A0A162MUK9_9FIRM
LinkDB: A0A162MUK9_9FIRM
Original site: A0A162MUK9_9FIRM 
ID   A0A162MUK9_9FIRM        Unreviewed;       812 AA.
AC   A0A162MUK9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Negative regulator of genetic competence ClpC/MecB {ECO:0000313|EMBL:KYO67382.1};
GN   Name=clpC {ECO:0000313|EMBL:KYO67382.1};
GN   ORFNames=ATZ99_06680 {ECO:0000313|EMBL:KYO67382.1};
OS   Thermovenabulum gondwanense.
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Thermosediminibacteraceae; Thermovenabulum.
OX   NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO67382.1, ECO:0000313|Proteomes:UP000075737};
RN   [1] {ECO:0000313|EMBL:KYO67382.1, ECO:0000313|Proteomes:UP000075737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R270 {ECO:0000313|EMBL:KYO67382.1,
RC   ECO:0000313|Proteomes:UP000075737};
RA   Patel B.K.;
RT   "Draft genome of Thermovenabulum gondwanense isolated from a red
RT   thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL   Submitted (DEC-2015) 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:KYO67382.1}.
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DR   EMBL; LOHZ01000022; KYO67382.1; -; Genomic_DNA.
DR   RefSeq; WP_068747823.1; NZ_LOHZ01000022.1.
DR   AlphaFoldDB; A0A162MUK9; -.
DR   STRING; 520767.ATZ99_06680; -.
DR   PATRIC; fig|520767.4.peg.756; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000075737; 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:SF18; HEAT SHOCK PROTEIN 104; 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:UP000075737};
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          415..450
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          411..457
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   812 AA;  91342 MW;  E72D253734A5EF05 CRC64;
     MNGKFTERAQ KVITYAQEEA RRLNHNVVGT EHLLLGLIRE GEGVAARALT NLGVDLQKVR
     EQVENLIGVG PFVIQGPIGY TPRAKRVLEL AMDESRRLKH NYVGTEHILL GLIREGEGVA
     AQVLNNLGVS LDRARNEVLS LLGTDVKGQA AFRRYNNTPT LNQFGRDLTE LAAEGKLDPV
     IGRQKEIERV IQVLTRRTKN NPCLIGEPGV GKTAIVEGLA QRIVEGDVPE ILKDKRIVSL
     DLALLVAGTK FRGEFEERLK KVLTEVKQAG NVILFIDEMH TLIGAGAAEG AIDASNILKP
     SLARGELQTI GATTLDEYRK HVEKDPALER RFQPIMVDEP TVEDTIKILE GLRDKYEAHH
     RVKISDEAIA AAAKLSSRYI TDRFLPDKAI DLIDEAASRV RLQCLTAPPE LKELEDELEA
     LRKEKDAAIR AQEFEKAAKL RDKEQDLKAK LDSLKSKWQS ENKLDNSTVT EADIAKIVSS
     WTGIPVERLT EEESERLLKM EDILHKRVIG QDEAVKAVAR AIRRARAGLK DPKRPIGSFI
     FLGPTGVGKT ELARALAEAM FGDENAMIRL DMSEYMEKFA VSRMIGAPPG YVGYEEGGEL
     TEKVRRRPYS VVLFDEIEKA HPDVFNILLQ ILEDGRLTDA QGRTVDFRNT IIIMTSNVGA
     NLIQKSRTFG FMPREEEEKN YNDMKDKVLE ELRRTFRPEF LNRVDEIIVF HALNETHIKE
     IVTLMLQQVN ERLKEFDIAI EVTDKAKEWL AKKGYDPMYG ARPLRRVIQR EIEDNLSEEL
     LKGTIAKGNT VLIDEKEGKL TFEKKELSIA SK
//
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