ID A0A3N2DC15_9MICO Unreviewed; 858 AA.
AC A0A3N2DC15;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:ROR97277.1};
GN ORFNames=EDD28_1874 {ECO:0000313|EMBL:ROR97277.1};
OS Salana multivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Salana.
OX NCBI_TaxID=120377 {ECO:0000313|EMBL:ROR97277.1, ECO:0000313|Proteomes:UP000275356};
RN [1] {ECO:0000313|EMBL:ROR97277.1, ECO:0000313|Proteomes:UP000275356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13521 {ECO:0000313|EMBL:ROR97277.1,
RC ECO:0000313|Proteomes:UP000275356};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:ROR97277.1}.
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DR EMBL; RKHQ01000001; ROR97277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2DC15; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000275356; Unassembled WGS sequence.
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; 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; PS50151; UVR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ROR97277.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:ROR97277.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:ROR97277.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000275356};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 423..458
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..465
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 858 AA; 94407 MW; E6080C35BAA10106 CRC64;
MFERFTDRAR RVVVLAQDEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SLGISLDVVR
QQVVDIIGEG QQAPTGHIPF TPRAKKVLEL SLREALQLGH NHIGTEHILL GLIREGEGVA
AQVLGNLGAD LGRVRQQVLQ LLQGQPGGGK ETVSAGGPQE GTPSGSAVLD QFGRNLTQLA
RENRLDPVIG RERETERVMQ VLSRRTKNNP VLVGEPGVGK TAVVEGLAQD IVRGTVPETL
KDKQLYTLDL GALVAGSRYR GDFEERLKKV LKEIRTRGDI ILFIDEIHTL VGAGAAEGAI
DAASILKPML ARGELQTIGA TTLDEYRKYV EKDPALERRF QPITVNEPTL AHAIEILKGV
RDRYEAHHRV TITDGALVAA ATLADRYVND RFLPDKAIDL VDEAGARLRI RRMTAPPELR
ELDERIAEAR RAKESAIDDQ DFEKAARLRD DEKNLTQERL EKEKAWKSGD MDTVATVDED
LIAEVLAVAT GIPVFKLTEE ESSRLLRMED ALHERIVGQK DAVKALSQAI RRTRAGLKDP
KRPGGSFIFA GPTGVGKTEL AKALAEFLFG DEDALIQLDM SEYGEKHTVS RLFGSPPGYV
GYEEGGQLTE KVRRRPFSVV LFDEVEKAHA DIFNSLLQIL EEGKLTDSQG RVVDFKNTII
IMTTNLGTRD IAKGVQTGFQ AGGDLSTDYE RMKSKVNDEL KQHFRPEFLN RVDDVVVFPQ
LSRDEIFQIV DLLVARLDKR LADRDMTIEL SEAAKTLLAD RGYDPVLGAR PLRRALQREI
EDALSEKILF GELRSGQKVL VDARGEGLLG EFTFVGVDRD DPRLDSSAIG EPEVVVVGAT
VADAPATPVE DAPSPSEG
//