ID A0A1C6SGN5_9ACTN Unreviewed; 847 AA.
AC A0A1C6SGN5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SCL28479.1};
GN ORFNames=GA0070624_3701 {ECO:0000313|EMBL:SCL28479.1};
OS Micromonospora rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=568872 {ECO:0000313|EMBL:SCL28479.1, ECO:0000313|Proteomes:UP000199413};
RN [1] {ECO:0000313|Proteomes:UP000199413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45431 {ECO:0000313|Proteomes:UP000199413};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-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}.
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DR EMBL; FMHV01000002; SCL28479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6SGN5; -.
DR STRING; 568872.GA0070624_3701; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199413; 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, ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:SCL28479.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SCL28479.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199413};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 34..180
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 443..478
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 164..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..485
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 847 AA; 94163 MW; E67984DF08500AA0 CRC64;
MRPGEFGPDP WDEFLARYFG RGEGGRRPPH RVDITRLMTA DAREMLADAA RRAAQRHSND
LDTDHLLWAA LQREPLRDLV RRAGADPDAL LNALGGRGDG APRGEVPPNL SLTPAAKRAL
LDAHQLSRAM GANYIGPEHI LMALPLNPES PAGRMLAAGR VQPESLQAAS AERGAGPRPD
RGTPTLDQYG RDLTDLARAD QIDPVIGRAD EIEQAVEILS RRTKNNPVLI GEAGVGKTAI
VEGLAERICD GDVPQTLLGK RVVQLDLAGL VAGTRYRGDF EERLKKVIDE IRAHKDELII
FLDEIHTLVG AGGAGAEGGM DASNMLKPAL ARGELRVIGA TTLDEYRRSI EKDAALARRF
QPVFVPEPTL EDTVAILRGL RDRYEAHHQV RFTDEALVAA AELSDRYITD RYLPDKAIDL
IDQAGARVRL RTRTPAEDVR DLERQLDEIR RNKAQAVSDE QYERASELRD RVSELEDQIR
RARGDGESPE VPTVGPTEIA EVVSRATGIP VAQLTEEERD RLLRLEGYLH ERVVGQDDAV
SAVAEAVRRS RTGLADPNRP MGSFLFLGPT GVGKTELARA LAEALFGESD RMVRVDMSEF
QERHTVSRLV GAPPGYVGYE EAGQLTEAVR RRPYAVVLLD EIEKAHPDVF NILLQVLDDG
RLTDSQGRTV NFKNTVLIMT SNLGSELITG AQRTVGFDLA QPGREQEASE LRERLLRRLQ
ENFRPEFLNR IDEVIVFQRL EAEQLRQITE LMLEETRRRL HAQDIQIEFT PAGIDWLAEH
GYQPEFGARP LRRVIQREVD NRVSRMLLEH QVSPGQKVVV DARDGQLVID VFAGDRDYAA
ASTSHPR
//