ID A0A1Q4WMB7_9ACTN Unreviewed; 846 AA.
AC A0A1Q4WMB7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Clp protease {ECO:0000313|EMBL:OKI11131.1};
GN ORFNames=AMK13_01340 {ECO:0000313|EMBL:OKI11131.1};
OS Streptomyces sp. CB02056.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703924 {ECO:0000313|EMBL:OKI11131.1, ECO:0000313|Proteomes:UP000186379};
RN [1] {ECO:0000313|EMBL:OKI11131.1, ECO:0000313|Proteomes:UP000186379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02056 {ECO:0000313|EMBL:OKI11131.1,
RC ECO:0000313|Proteomes:UP000186379};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI11131.1}.
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DR EMBL; LIPD01000001; OKI11131.1; -; Genomic_DNA.
DR RefSeq; WP_074000790.1; NZ_LIPD01000001.1.
DR AlphaFoldDB; A0A1Q4WMB7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000186379; 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 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.
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:OKI11131.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OKI11131.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186379};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 36..179
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 173..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 446..492
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 846 AA; 92217 MW; AB535708F354F666 CRC64;
MTMPPFGSND PFSDLLSRFF GMSPMASPPA VQRVPIGRLL SESSQELLAL AAQRAAEDGS
SDLDTAHLAW AATRVDPSRR MLERAGIDPD RLSGDLEHAL PSGNPETVDG RPALTPSAKR
ALLAAHARSQ EAGASYIGPE HILGALLDQE RSGAGVALRN AAPSQEALKS VLEGRGTGGE
RSSTGAHPSE TPTLDEYGRD LTEEARSGRL DPVVGRAEEI EQTVEILSRR TKNNPVLIGE
PGVGKTAIVE GLAQRIVSGD VPQSLREKRV VTLDLTALVA GSKYRGEFEE RLKNVIDEVT
AAEKSVILFL DELHTVVGAG GGGEGSMDAG NILKPALARG ELSVVGATTL DEYRKHVEKD
AALERRFQPV LVPEPSVEET IEILQGLRDA YEAHHQVRFT DEALDAAATL SDRYVSDRFL
PDKAIDLLDQ AGARVRLRSL SGSTEATGVR DRITKLKREL DEAVADEEFV RAANLKTELR
QTEDELAAVA ESREEVVDVT ADDIAQVLSS RTGIPVAELN ATEKERLLKL EDHLHQKVIG
QDEAVTAVSQ AVRRGRAGMG DPERPTGSFL FLGPTGVGKT ELAKALAALL FGDPDRMIRF
DMSEFQEKHT VSRLVGSPPG YVGYEEAGQL TEAVRRKPYS VLLFDEVEKA HPDVFNLLLQ
VLDDGRLTDS QGRTVDFRNT VVIMTSNIGS QRILDHAGNV DEIRDDLMRD LRQHFRPEFL
NRIDEVIVFH ALTRKDLLSV VDLLLERSRR RLRAQDIRLE VTEAAKEYLV NRGYQPEFGA
RPLRRTIQSE LDNRISNLLL DGSVREGDTL IAEVSDGELV VTLARPEASA TFEEAEAKAA
AAAAEG
//