ID A0A3G8JM23_9ACTN Unreviewed; 848 AA.
AC A0A3G8JM23;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC1 {ECO:0000313|EMBL:AZG46043.1};
GN Name=clpC1_1 {ECO:0000313|EMBL:AZG46043.1};
GN ORFNames=D7316_02643 {ECO:0000313|EMBL:AZG46043.1};
OS Gordonia insulae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=2420509 {ECO:0000313|EMBL:AZG46043.1, ECO:0000313|Proteomes:UP000271469};
RN [1] {ECO:0000313|EMBL:AZG46043.1, ECO:0000313|Proteomes:UP000271469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS17-SY073 {ECO:0000313|EMBL:AZG46043.1,
RC ECO:0000313|Proteomes:UP000271469};
RA Kim Y.S., Kim S.B.;
RT "Gordonia insulae sp. nov., isolated from an island soil.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP033972; AZG46043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8JM23; -.
DR KEGG; gom:D7316_02643; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000271469; Chromosome.
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:AZG46043.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AZG46043.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:AZG46043.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000271469};
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 425..460
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 814..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 421..467
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 814..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 93890 MW; 19F61F7B196BC74B CRC64;
MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SLGISLEGVR
SQVEEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
AQVLVKLGAD LNRVRQQVIQ LLSGYQGKEP QEAGTGGRST EAGTPSTSLV LDQFGRNLTA
AAGEGKLDPV IGREKEIERV MQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QAIVNGQVPE
TLKDKQLYTL DLGSLVAGSR YRGDFEERLK KVLKEINTRG DIILFIDELH TLVGAGAAEG
AIDAASILKP KLARGELQTI GATTLDEYRK YIEKDAALER RFQPVQVGEP SVEHTIEILK
GLRDRYESHH RVSITDGALV AAATLADRYI NDRFLPDKAI DLIDEAGARM RIRRMTAPPD
LREFDDRIAD ARKEKESAID AQDFEKAANL RDKEKQLVAE RAEREKQWRS GDMDVVAEVD
DEQIAEVLGN WTGIPVFKLT EEETTRLLRM EDELHKRIIG QEDAVKAVSK AIRRTRAGLK
DPKRPSGSFI FAGPSGVGKT ELSKALANFL FGEDDALIQI DMGEFHDRFT ASRLFGAPPG
YVGYEEGGQL TEKVRRKPFS VVLFDEIEKA HSEIYNTLLQ VLEDGRLTDG QGRTVDFKNT
VLIFTSNLGT GDISKAVGLG FTQGGSDGSQ YERMKQKVND ELKKHFRPEF LNRIDDVIVF
HQLTRDEIIQ MVDLMINRVE TQLKNKDMAI ELTDQAKALL AKRGFDPVLG ARPLRRTIQR
EIEDQLSEKI LFNEIGAGQI ILVDVEGWDG EDDGEDAKFV FTGSDKPREV PDAPAELTKA
GDSKGEAS
//