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Database: UniProt
Entry: A0A1R4FRQ6_9ACTO
LinkDB: A0A1R4FRQ6_9ACTO
Original site: A0A1R4FRQ6_9ACTO 
ID   A0A1R4FRQ6_9ACTO        Unreviewed;       859 AA.
AC   A0A1R4FRQ6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpC / Negative regulator of genetic competence clcC/mecB {ECO:0000313|EMBL:SJM58616.1};
GN   ORFNames=CZ771_10375 {ECO:0000313|EMBL:SJM58616.1};
OS   Actinomycetales bacterium JB111.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales.
OX   NCBI_TaxID=1434822 {ECO:0000313|EMBL:SJM58616.1, ECO:0000313|Proteomes:UP000196124};
RN   [1] {ECO:0000313|EMBL:SJM58616.1, ECO:0000313|Proteomes:UP000196124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB111 {ECO:0000313|EMBL:SJM58616.1,
RC   ECO:0000313|Proteomes:UP000196124};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUHX01000052; SJM58616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4FRQ6; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000196124; 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:SJM58616.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SJM58616.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196124};
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          421..456
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          832..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  94926 MW;  5D1021E38411CFBD CRC64;
     MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE ALDISLEAVR
     AQVTEIIGEG QQAPQGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
     AQVLTKLGAD LNRVRQQVIQ LLSGYQGKEA VAAGGPAEGQ PSGSAVLDQF GRNLTQAARE
     GRLDPVIGRA EQIERVMQVL SRRTKNNPVL IGEPGVGKTA VVEGLAQDIV RGDVPETLKD
     KQLYTLDLGS LVAGSRYRGD FEERLKKVLK EIRTRGDIVL FIDEIHTLVG AGAAEGAIDA
     ASILKPMLAR GELQTIGATT IDEYRKHIEK DAALERRFQP IQVPEPSVEH AVEILKGLRD
     RYEAHHRVSI TDEALAAAVT LADRYVSDRH LPDKAIDLID EAGARLRIRR MTAPPELREL
     DEQIEEVRRE KESAIDDQDF EKAASLRDDE HRLGERRAER EKAWREGDLD EVSEVDEELV
     AEVLAMSTGI PVVKLTEEES QKLLHMEDEL HKRIIGQDEA ISTLSQAIRR TRSGLKDPRR
     PGGSFIFAGP TGVGKTELAK ALAEFLFGDE DALITLDMSE YSEKHTVSRL FGAPPGYVGY
     EEGGQLTEKV RRRPFSVVLF DEVEKAHQDL FNSLLQILED GRLTDSQGRV VDFKNTVIIM
     TTNLGTKDIA KGVQTGFQAT GALSSSYERM KAKVNEELKQ HFRPEFLNRV DDTIVFPQLT
     QDQIVKIVDL MIARLDERLR DQEMTIELTD AAKELLAERG YDPVLGARPL RRAIQRDIED
     VLSEKILFGE VKAGQIIKVD ASGEGILGEL TFTFEEHDGP ILKATKADAD RYAQSAGRQL
     PPAVPVGGAG GSGQMQPGS
//
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