ID A0A1H1SJL0_9ACTN Unreviewed; 841 AA.
AC A0A1H1SJL0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SDS48175.1};
GN ORFNames=SAMN04489812_2040 {ECO:0000313|EMBL:SDS48175.1};
OS Microlunatus soli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=630515 {ECO:0000313|EMBL:SDS48175.1, ECO:0000313|Proteomes:UP000199103};
RN [1] {ECO:0000313|EMBL:SDS48175.1, ECO:0000313|Proteomes:UP000199103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21800 {ECO:0000313|EMBL:SDS48175.1,
RC ECO:0000313|Proteomes:UP000199103};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
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; LT629772; SDS48175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1SJL0; -.
DR STRING; 630515.SAMN04489812_2040; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199103; Chromosome i.
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:SDS48175.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDS48175.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199103};
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 422..457
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 806..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 93082 MW; 963EA8B465F0BAED CRC64;
MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SMGISLEAVR
EKVEEIIGHG HESPSGHIPF TPRAKKVLEL SLREALQINH SYIGTEHILL GLIREGEGVA
AQVLVKLGAD LNRVRQTVLQ LLSGFQGKEA ATSGAPEQGN APSSSMVLDQ FGRNLTQAAR
ENKLDPVIGR ETEIERVMTV LSRRTKNNPV LIGDPGVGKT AVVEGLAQSI VRGDVPETLR
DKQIYTLDLG ALVAGSRYRG DFEERLRKVL KEIKTRGDVV LFIDEIHTLV GAGAAEGAID
AASILKPMLA RGELQTIGAT TLDEYRKYVE KDAALERRFQ PIQVAEPSIA LTIDILRGLR
DRYEAHHRIT ITDEALVGAA RMADRYISDR FLPDKAIDLI DEAGARLRIR RMTAPPDLRE
FDEKIAAVRL EKEAAIDAQD FERAAGLRDD EKKLLAQRAE RESQWKQGDL DAVAEVDEEI
IAEVLSTTTG IPVFKLTEEE SSRLLRMEQE IAKRYVGQDD AVKALSRSIR RTRAGLKDPK
RPSGSFIFAG PSGVGKTELT KALTEFLFED EDAMITLDMS EYSEKHTASR LFGSPPGYVG
YEEGGQLTEK VRRKPFSVVL FDEIEKAHPD IFNSLLQILD EGRLTDAQGR VVDFKNTVIV
MTTNLGTRDI AKSVTLGFSQ AGDAEGSYEK MKAKVSDELK QHFRPEFLNR VDEIIVFRQH
GMDDIVKIVD LMVNEIEERL KDKDMDIELT PAAKQLVAKR GFDPVLGARP LRRALQRDVE
DVLAEKILFD ELKAGEIVVV DVAPEGSEDP FTFTGTPRAE VPDTPVSVGA GPDEGTESNA
S
//