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Database: UniProt
Entry: A0A160F2U3_9BACI
LinkDB: A0A160F2U3_9BACI
Original site: A0A160F2U3_9BACI 
ID   A0A160F2U3_9BACI        Unreviewed;       810 AA.
AC   A0A160F2U3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Negative regulator of genetic competence ClpC/MecB {ECO:0000313|EMBL:ANB60566.1};
GN   Name=clpC {ECO:0000313|EMBL:ANB60566.1};
GN   ORFNames=GFC30_103 {ECO:0000313|EMBL:ANB60566.1};
OS   Anoxybacillus amylolyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB60566.1, ECO:0000313|Proteomes:UP000076865};
RN   [1] {ECO:0000313|EMBL:ANB60566.1, ECO:0000313|Proteomes:UP000076865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB60566.1,
RC   ECO:0000313|Proteomes:UP000076865};
RX   PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA   Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA   Gambacorta A., Nicolaus B.;
RT   "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT   bacterium isolated from Mount Rittmann (Antarctica).";
RL   Syst. Appl. Microbiol. 29:300-307(2006).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP015438; ANB60566.1; -; Genomic_DNA.
DR   RefSeq; WP_066322120.1; NZ_CP015438.1.
DR   AlphaFoldDB; A0A160F2U3; -.
DR   KEGG; aamy:GFC30_103; -.
DR   PATRIC; fig|294699.3.peg.95; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000076865; 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:UP000076865};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          417..452
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          413..463
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   810 AA;  90345 MW;  9727CBD87242A7B7 CRC64;
     MMFGRFTERA QKVLALAQEE AVRLGHNNIG TEHILLGLIR EGEGIAAKAL IALGLGPDKI
     QKEVEALIGR GHESSQTIHY TPRAKKVIEL SMDEARKLGH SYVGTEHILL GLIREGEGVA
     ARVLNNLGVS LNKARQQVLQ LLGSNESISG HQGSASHVST PTLDSLARDL TAIAREGSLD
     PVIGRSKEIQ RVIEVLSRRT KNNPVLIGEP GVGKTAIAEG LAQQIVNNEV PETLRDKRVM
     TLDMGTVVAG TKYRGEFEDR LKKVMDEIRQ AGNIILFIDE LHTLIGAGGA EGAIDASNIL
     KPSLARGELQ CIGATTLDEY RKYIEKDAAL ERRFQPIYVD EPTVEESIQI LKGLRDRYEA
     HHRVSISDEA IVQAVKLSDR YITDRFLPDK AIDLIDEACS KVRLRSFTTP PNLKELEQKL
     EEVRKEKDAA VQSQEFEKAA SLRDTEQRLR EQLEETKRAW KEKQGKENSE VTVEDIAMVV
     SSWTGIPVSK LAQTETERLL KLEEILHSRV IGQEEAVKAV AKAVRRARAG LKDPKRPIGS
     FIFLGPTGVG KTELARALAE AMFGDEDALI RIDMSEYMEK HSTSRLVGSP PGYVGYEEGG
     QLTEKVRRKP YSVVLLDEME KAHPDVFNIL LQVLEDGRLT DSKGRTVDFR NTIVIMTSNV
     GADALKRHKY VGFNVQDESE KYKDMKGKVM EELKKAFRPE FLNRIDEIIV FHALEKPHLA
     QIVNLMAEQL VKRLKEQDID LELTQAAIEK IAAEGYDPEY GARPLRRALQ KHIEDRLSEE
     LLKGTIAKGQ KVVVDVKDGE FVVLSEQTVQ
//
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