ID A0A3D9LFK9_9MICC Unreviewed; 845 AA.
AC A0A3D9LFK9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:REE04630.1};
GN ORFNames=C8E99_2470 {ECO:0000313|EMBL:REE04630.1};
OS Citricoccus muralis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Citricoccus.
OX NCBI_TaxID=169134 {ECO:0000313|EMBL:REE04630.1, ECO:0000313|Proteomes:UP000256727};
RN [1] {ECO:0000313|EMBL:REE04630.1, ECO:0000313|Proteomes:UP000256727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14442 {ECO:0000313|EMBL:REE04630.1,
RC ECO:0000313|Proteomes:UP000256727};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUL-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:REE04630.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QREH01000001; REE04630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9LFK9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000256727; 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:SF175; ATP-DEPENDENT CLP PROTEASE, ATP-BINDING SUBUNIT CLPC; 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};
KW Hydrolase {ECO:0000313|EMBL:REE04630.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:REE04630.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000256727};
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 429..464
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 445..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 92986 MW; 2D04736E25FF7061 CRC64;
MFERFTDRAR RVVVLAQEEA RMLNHSYIGT EHILLGLIHE GEGVAAKALE SLNISLGAVR
EQVQEIIGQG QQTPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
AQVLVKLGAD LNRVRQTVIQ LLSGYQGGAG GKETAGAGVS AGGQSEGAPA GSVVLDQFGR
NLTAAAREGK LDPVIGRALE MERVMQVLSR RTKNNPVLIG EPGVGKTAVV EGLAQAIVRN
DVPETLMDKQ LYTLDLGSLV AGSRYRGDFE ERLKKVLKEI RTRGDIILFI DEIHTLVGAG
AAEGAIDAAS ILKPMLARGE LQTIGATTLD EYRKHIEKDA ALERRFQPIQ VNEPSVEETT
EILRGLRDRY EAHHRVSITD EALKSAATLA DRYVSDRFLP DKAIDLIDEA GARLRIKRMT
TPPEIKEFEA RIAEVRAEKE AAIDGQDFEG AANLRDQEQK LTDERNQKEE EWRTSVTEGI
AEVDDDLIAE VLSTSTGIPV FKLTEEETDR LRNMEAELHQ RVIGQNEAIK SLSQAIRRTR
AGLKDPNRPS GSFIFAGPTG VGKTELAKAL AEFLFGDEEA LITLDMSEFQ EKHTVSRLFG
APPGYVGYEE GGQLTEKVRR RPFSVVLFDE VEKAHADLFN SLLQILEDGR LTDSQGRVVD
FKNTVIIMTT NLGTKDISKG VMTGFQSAAD TQTGYDRMKG KVQEELRQHF RPEFLNRVDD
VIVFPQLSRG EIVQIVDLFI ARLQKRLDEQ DLTISVSTPA KEFLANRGYD PAMGARPLRR
TIQHLVEDQL SERILFGEIT PGSAISVGLE GEAETAKLTF TIAHQPEALE AAPEHGEIEA
SAPGQ
//