GenomeNet

Database: UniProt
Entry: A0A3M0ICW1_9ACTN
LinkDB: A0A3M0ICW1_9ACTN
Original site: A0A3M0ICW1_9ACTN 
ID   A0A3M0ICW1_9ACTN        Unreviewed;       825 AA.
AC   A0A3M0ICW1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Clp protease {ECO:0000313|EMBL:RMB85890.1};
GN   ORFNames=CTZ28_10235 {ECO:0000313|EMBL:RMB85890.1};
OS   Streptomyces shenzhenensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=943815 {ECO:0000313|EMBL:RMB85890.1, ECO:0000313|Proteomes:UP000270471};
RN   [1] {ECO:0000313|EMBL:RMB85890.1, ECO:0000313|Proteomes:UP000270471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=193 {ECO:0000313|EMBL:RMB85890.1,
RC   ECO:0000313|Proteomes:UP000270471};
RA   Siqueira K.A., Liotti R.G., Mendes T.A.O., Soares M.A.;
RT   "Draft genome of actinobacteria isolated from guarana (Paullinia cupana
RT   (Mart.) Ducke.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:RMB85890.1}.
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; PENI01000005; RMB85890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0ICW1; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000270471; Unassembled WGS sequence.
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 78, MITOCHONDRIAL; 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:RMB85890.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RMB85890.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000270471};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          41..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          94..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          439..485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        172..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   825 AA;  90333 MW;  1B593F247EEF3BDE CRC64;
     MTTPGFGFGR SPFEEFDELM SRFFGGTGQA APARRIQRVD IGSLLSERGR ELVAEARDIA
     AAEGSEDLDA RQLLAAATEH DSTRRLISEA GADPDGIRER LGTAAGSGAK TEPATLTPAA
     KRALLDAYQL SRAEGASYIG PEHLLRALAA NPESAAGRVL AESGWEPTRM PTETAAERRR
     PSSTPTLDEY GRDLTEDARA GRLDPVIGRD DEVEQTIEVL SRRSKNNPVL IGDPGVGKTA
     IVEGIAQRIT AGDVPQTLKD KRLVSLDLAG LVAGTKYRGE FEERLKKLLD EVGEHGDELV
     LFLDELHTVV GAGGGGEGAL DAGNMLKPAL ARGELHLIGA TTVDEYRKHI EKDAALERRF
     APILVGEPTV DDTIAILHGL RDRYEAHHQV RITDEAVVAA AELSDRYITS RFLPDKAIDL
     MDQAAARVRL RAKTPLADTR DVEDRIAALN REKDQAVADE EYERAKELRD RIKEAETRLA
     EAAKEEKRTP EVTAEDIAEV VSRTTGIPVA QLTEEERERL MKLEEHLHER VVGQDEAITA
     VARAVRRARA GMSDPNRPVG SFLFLGPTGV GKTELARALA AALFGDDSRM IRLDMSEFQE
     RHTVSRLVGA PPGYIGHEEA GQLTEAVRRQ PYAVLLLDEV EKAHPDVFNT LLQLLDDGRL
     TDSQGRTVDF KNTVVIMTSN IGADRILAAG VEDYTKVRES VMPVLHQRFR PEFLNRIDEI
     IVFRGLDRAQ LRQIVDLLLE HTRRRLHAQE VGLEVTDEAA ALLANIGYQP DFGARPLRRT
     IQREVDDRLA DLLLSGRLSA GDRAVVDAAE GSVTIRADKP AGVAD
//
DBGET integrated database retrieval system