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}.
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; 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
//