ID A0A1S2PX35_9ACTN Unreviewed; 838 AA.
AC A0A1S2PX35;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Clp protease {ECO:0000313|EMBL:OIJ98389.1};
GN ORFNames=BIV24_05960 {ECO:0000313|EMBL:OIJ98389.1};
OS Streptomyces colonosanans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428652 {ECO:0000313|EMBL:OIJ98389.1, ECO:0000313|Proteomes:UP000179935};
RN [1] {ECO:0000313|EMBL:OIJ98389.1, ECO:0000313|Proteomes:UP000179935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 93 {ECO:0000313|EMBL:OIJ98389.1,
RC ECO:0000313|Proteomes:UP000179935};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 93.";
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 -!- 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:OIJ98389.1}.
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DR EMBL; MLYP01000013; OIJ98389.1; -; Genomic_DNA.
DR RefSeq; WP_071365091.1; NZ_MLYP01000013.1.
DR AlphaFoldDB; A0A1S2PX35; -.
DR STRING; 1428652.BIV24_05960; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000179935; 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:OIJ98389.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OIJ98389.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179935};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 36..176
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 439..474
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 152..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 90665 MW; 593AB699CDF1D8A4 CRC64;
MTISPFGSGD PFSELFNRFF GMSPATSPPA VQRVPIGRLL SGSSQELLAA AGGRAAEDGS
DLDTVHLLWA ATQVPAARQL LEQAGADPDR LAADLQESLP TGTGTGEPAL TPAAKRALLA
AHARSQAAGA SYIGPEHILA ALLDDPRSPL TQTLRAEGAS PGALSGPARE GRPAGGHPDT
PTLEQYGRDL TDEARSGRLD PVVGRAGEIE QTIEVLSRRT KNNPVLIGDP GVGKTAIVEG
LAQRIVAEEV PKALKNRRVA ALEMAGLVAG SQYRGQFEER LKKVIDEVTQ AQKGIILFID
ELHTVVGAGG TGEGSMDAGN ILKPALARGD LSVVGATTID EYRKHIEKDA ALERRFQPVM
VPEPTVEETI EILRGLRDSY EAHHQVRYTD EALDAAASLS DRYISDRFLP DKAIDLMDQA
GARVGLRSVG GSREAAELED RLSRLRREKD EAVSTEDFTR AGELKREVTE LEERLGSMGE
GGVPTPAVTP EDIAEVLSAR TGIPVSQLTE TERERLLKLE EVLHERVIGQ DQAVTAVAQA
VRRGRAGMGD PDRPTGSFLF LGPTGVGKTE LAKALAELLF GDPDRMVRFD MSEFQEKHTV
SRLIGSPPGY VGYEEAGQLT EAVRRKPYSV VLFDEVEKAH RDVFNLLLQV LDDGRLTDAK
GRTVDFRNTV VIMTSNIASK RILDHHGDVE EIKDDLMAEL QAHFRPEFLN RIDEVIVFHA
LVREDLVRIV DLLLEGSRRR LHAQQVGLEV TEAAKDWLAE RGYQPEYGAR PLRRTIQSEL
DNRLSNMLLD GTLNPGDTVV ADVADDELVL GLKAKPATDD KAAPGEGGAQ GSPEGCER
//