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Database: UniProt
Entry: A0A495JVF7_9ACTN
LinkDB: A0A495JVF7_9ACTN
Original site: A0A495JVF7_9ACTN 
ID   A0A495JVF7_9ACTN        Unreviewed;       854 AA.
AC   A0A495JVF7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:RKR92548.1};
GN   ORFNames=BDK92_6989 {ECO:0000313|EMBL:RKR92548.1};
OS   Micromonospora pisi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR92548.1, ECO:0000313|Proteomes:UP000277671};
RN   [1] {ECO:0000313|EMBL:RKR92548.1, ECO:0000313|Proteomes:UP000277671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR92548.1,
RC   ECO:0000313|Proteomes:UP000277671};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, 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:RKR92548.1}.
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DR   EMBL; RBKT01000001; RKR92548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495JVF7; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000277671; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:RKR92548.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RKR92548.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277671};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          35..180
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          449..484
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          90..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          445..491
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        838..854
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   854 AA;  94333 MW;  78175BAF787ACBD6 CRC64;
     MTQPPGDSGV DPWDEFLARY FGRGEGRRPA HRVDITRLMT ADARELLADA ARRAASASSS
     DLDTDHLLWA ALQREPLREL VRRAGADPDA LAGALGGQQR QAEPAPHGQV PPNLSLTPAA
     KRALLDAHQL SRAMGASYIG PEHILMALPL NPESPAGRML AAGRIQPQAL QNANSERSGA
     PTPKPDRGTP TLDQYAQDLT DLARADEIDP VIGRADEIEQ AVEILSRRTK NNPVLIGEAG
     VGKTAIVEGL AERIADGDVP RTLLGKRVVQ LDLAGLVAGT RYRGDFEERL KKVIDEIRAH
     GEELIVFLDE LHTLVGAGGA GSEGGMDASN MLKPALARGE LRVVGATTLN EYRRYIEKDA
     ALARRFQPVL VPEPSVDDTV AILRGLRDRY EAHHQVRFTD EALVAAAELS DRYLTDRFLP
     DKAIDLLDQA GARVRLRTRT PDSDVRDLER ELEDLRRDKE QAVADEQYER ASQLRDRLQN
     VQEQIEASRG DNGRNQVPEV RPQEIAEVVS RATGIPVSQL TEEERDRLLR LEGHLHERIV
     GQDDAVNAVA EAVRRSRTGL ADPDRPMGSF LFLGPTGVGK TELARALAEA LFGESDRMIR
     LDMSEFQERH TVSRLVGAPP GYVGYEEAGQ LTEAVRRRPY AVVLLDEIEK AHPDVFNILL
     QVLDDGRLTD SQGRTVNFRN TVLIMTSNLG SELITGTQRS VGFGGDGAEE ESAELRERLM
     RRLQEHFRPE FLNRIDEVII FRRLESEQLR QITELLLEET RQRLHAQDIV VDFTTPGVDW
     IAEHGYQPEF GARPLRRTIQ REIDNRLSRM LLDGSLAPGQ RITIDAADGA LTFDVSDSGR
     GSGRNPTPAS ASAE
//
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