ID E2Q1R3_STRCL Unreviewed; 860 AA.
AC E2Q1R3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Chaperone {ECO:0000313|EMBL:EFG10689.1};
GN ORFNames=SCLAV_5622 {ECO:0000313|EMBL:EFG10689.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG10689.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG10689.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
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}.
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DR EMBL; CM000913; EFG10689.1; -; Genomic_DNA.
DR AlphaFoldDB; E2Q1R3; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000002357; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000002357};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 39..179
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 440..475
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 153..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..489
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 860 AA; 92409 MW; 5A4D9CFB8BFDE266 CRC64;
MTAVTTSPFG SGDPFSDLFN RFFGMSPAAS PPAVQRVPIG RLLSDSAQEL LAAAGARAAE
DGSDLDTPHL LWAATRVPAG RQVLEQAGVD PDALADRVGR SLPTGTGAGE PALTPAAKRA
LLAAHARSQA LGASYIGPEH ILAALADDPA SGFTGALPSG GPGGDPGTGE RHARAGGGSP
TPTLDEYGRD LTEEARAGRL DPVVGRAQEI EQTVEILSRR TKNNPVLIGD PGVGKTAIVE
GLAQRVVADE VPRALKDRRV VSLDLAGLVA GSKYRGEFEE RLKKVIDEVT AADKSVVLFI
DELHTVVGAG GGGEGSMDAG NILKPALARG DLSVVGATTI DEYRKHIEKD AALERRFQPV
MVPEPTVEET VEILQGLRDS YEIHHQVRFT DEALDAAAAL SDRYLSDRFL PDKAIDLMDQ
AGARVGLRAV GTPDRNHDLE DRVTKLRREK DEAVSSEDYE RAGALKARLR AAEEELAQVG
EEREQTADVT AEDIAEVLSA RTGIPVSQLT ETERHRLMKL EDALHERVIG QDEAVVAVSQ
AVRRGRAGMG DPDRPTGSFL FLGPTGVGKT ELAKALAQLL FGDADRMIRF DMSEFQEKHT
VSRLVGSPPG YVGYEEAGQL TEAVRRKPYS VVLFDEVEKA HPDVFHLLLQ VLDDGRLTDA
QGRTVDFRHT VVIMTSNIGS KRILDHHGAV DEIRDDLMGD LRAHFRPEFL NRIDEVIVFH
ALTRDDLIHI VDLLLEGTRR RLHAQRVGFE ITEAAKERLA NLGYQPEFGA RPLRRTLQTE
LDNRLSTMLL DGTLSPGDTV VADVRDGGLT LSLKQPDPTA DDPAADPAAD PSAEPSPEPS
AEPEKDGKGR SGEAGTEAGN
//
