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Database: UniProt
Entry: A0A542ZCV2_9ACTN
LinkDB: A0A542ZCV2_9ACTN
Original site: A0A542ZCV2_9ACTN 
ID   A0A542ZCV2_9ACTN        Unreviewed;       841 AA.
AC   A0A542ZCV2;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:TQL58121.1};
GN   ORFNames=FB460_1974 {ECO:0000313|EMBL:TQL58121.1};
OS   Propioniferax innocua.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propioniferax.
OX   NCBI_TaxID=1753 {ECO:0000313|EMBL:TQL58121.1, ECO:0000313|Proteomes:UP000316196};
RN   [1] {ECO:0000313|EMBL:TQL58121.1, ECO:0000313|Proteomes:UP000316196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8251 {ECO:0000313|EMBL:TQL58121.1,
RC   ECO:0000313|Proteomes:UP000316196};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (JUN-2019) 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:TQL58121.1}.
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DR   EMBL; VFOR01000002; TQL58121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A542ZCV2; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000316196; 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};
KW   Hydrolase {ECO:0000313|EMBL:TQL58121.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TQL58121.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000316196};
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          426..461
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          150..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          820..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   841 AA;  92852 MW;  BE092ECD1CC20731 CRC64;
     MFERFTDRAR RVVVLAQDEA RNLNHNYIGT EHILLGLIAE GEGVAARALE SMDISLDAVR
     EQVEEIIGHG QQSPTGHIPF TPRAKKVLEL SLREALQLNH QYIGTEHILL GLIREGEGVA
     AQVLVKLGAD LGRVRNTVLQ LLSGFQGGKG EGAAVGGGPS DQGQGPGSST VLDQFGRNLT
     QAARENNLDP VIGREREIER VMTVLSRRTK NNPVLIGEPG VGKTAVVEGL SQAIVRGDVP
     ETLRDKQIYT LDLGALVAGS RYRGDFEERL KKVLKEIRTR GDVVLFIDEI HTLVGAGAAE
     GAIDAASILK PMLARGELQT IGATTLDEYR KHIEKDAALE RRFQPIQVDE PTIPQTVDIL
     KGLRDRYEAH HRITITDAAL SAAAQMADRY IQDRFLPDKA IDLIDEAGAR LRIKRMTAPP
     DLREFDEKIA TVRLEKEAAI DAQDFEKAAG LRDDEKKLLA ERAEKEQAWK AGDSDTAAEV
     DEETIAEVLS SATGIPVFKL TEEESQRLLH MEDELHKRYV GQVDAVAALS RSIRRTRAGL
     KDPKRPSGSF IFAGPSGVGK TELTKALTEF LFGDEEALIT LDMSEYSEKH TASRMFGSPP
     GYVGYEEGGQ LTEKVRRKPF SVVLFDEIEK AHPDIFNSLL QILDEGRLSD AQGRVVDFKN
     TVIVMTTNLG TRDISKSVNL GFSQSTDTES TYERMKSKVS EELKGHFRPE FLNRVDEIVV
     FRQLTQENIE NIVDLMVAQV EERLRDKDMG IELTQEARKL IAKRGFDPVL GARPLRRALQ
     RDVEDVLAEK ILFGEFGAGE IILVDVNEGE NATEEPFTFT STRPAAAPDE IPAELTGGDD
     A
//
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