ID A0A1H5BC59_9MICO Unreviewed; 841 AA.
AC A0A1H5BC59;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SED51664.1};
GN ORFNames=SAMN04488554_0058 {ECO:0000313|EMBL:SED51664.1};
OS Ruania alba.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae; Ruania.
OX NCBI_TaxID=648782 {ECO:0000313|EMBL:SED51664.1, ECO:0000313|Proteomes:UP000199220};
RN [1] {ECO:0000313|Proteomes:UP000199220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21368 {ECO:0000313|Proteomes:UP000199220};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNTX01000001; SED51664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5BC59; -.
DR STRING; 648782.SAMN04488554_0058; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199220; 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:SF155; CLP PROTEASE ATP-BINDING SUBUNIT; 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:SED51664.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:SED51664.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SED51664.1};
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 421..456
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 817..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 92823 MW; E2F5387AA20DE57C CRC64;
MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SLNISLEAVR
QQVQEIIGEG QQAPNGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
AQVLTKLGAD LNRVRQQVIQ LLNGYQGKEA VSAGGPAEGT PSGSAVLDQF GRNLTQAARE
SKLDPVIGRK PEVERVMQVL SRRTKNNPVL IGEPGVGKTA VVEGLAQDIV RGDVPETLKD
KQLYTLDLGA LVAGSRYRGD FEERLKKVLK EIRTRGDIIL FIDEIHTLVG AGAAEGAIDA
ASILKPMLAR GELQTIGATT LDEYRKHIEK DAALERRFQP IQVAEPTLTH AIEILKGLRD
RYEAHHRVTI TDAALVAAAN LADRYVNDRF LPDKAIDLID EAGARLRIRR MTAPPELREL
DDQIAETRRA KESAIDDQDF EKAARLRDEE KTLSNTRLEK EKAWKAGDMD NVAEVDEELI
AEVLAASTGI PVFKLTEEES SRLLRMEDEL HKRIVGQNAA VKAISQAIRR TRAGLKDPKR
PGGSFIFAGP TGVGKTELAK ALAEFLFGDE DALIQLDMSE FSEKHTVSRM FGSPPGYVGY
EEGGQLTEKV RRRPFSVVLF DEVEKAHADI FNSLLQILED GRLTDSQGRV IDFKNTVIIM
TTNLGTRDIA KGLLTGFQAG GDLSTNYDRM KVKVNEELKQ HFRPEFLNRV DDVIVFPQLS
QDEIFQIVDL MVAKLSVRLA DKDMDLELTP AAKELIAERG YDPVLGARPL RRALQREIED
QLSERILYGE IRAGQTVVVD ATGEGLLGEF TFTGVDREPE KEPLAVGAGG SPELPAATSG
E
//