ID A0A0B5EXM5_STRA4 Unreviewed; 870 AA.
AC A0A0B5EXM5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Chaperone {ECO:0000313|EMBL:AJE87568.1};
GN ORFNames=SLNWT_7192 {ECO:0000313|EMBL:AJE87568.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE87568.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE87568.1, ECO:0000313|Proteomes:UP000031523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC {ECO:0000313|Proteomes:UP000031523};
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; CP010519; AJE87568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5EXM5; -.
DR STRING; 1888.Salbus254_3034; -.
DR KEGG; sals:SLNWT_7192; -.
DR Proteomes; UP000031523; 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 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.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000031523};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 38..180
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 820..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 94261 MW; 4112ECAA80E82835 CRC64;
MSMSSFGLGS SDPFSDLLNR FFGTSPASSP PAVQRVPIGR LLTESSHELL NLAARRALED
GTSDLDTEHL LWAATKVDPA RALLAQAGAD PDTLAARIAE VLPRESGEPS AQPDLTPAAK
RVLAAAYARS QAAEVSYIGP EHILGALLDD TDTGAARLLG AEGQDVRKLA GLTEQAARAD
GAPGEVKQPA TTLDEFGRDL TEEAKAGKLD PVVGRAEEIE QTVEVLSRRS KNNPVLIGEP
GVGKTAIVEG LAQRIVAGEV PDTLKDKRVV ALDLSGMVAG AQYRGQFEER LKKVIEEVQN
ARGDIVLFID ELHTVVGAGA TGEGSMDAGN MLKPALARGE LHVVGATTID EYRRDIEKDA
ALERRFQPVL VPEPTVEETV QILEGLRDAY EAHHQVRFAD GALASAAELS DRYISDRFLP
DKAIDVMDQA GARVRLRSAS RSTEVVSRED RLARLRREQD QAVAAEDFDR AGQLKREIAE
AEGELAGVEE RRAGVVSVTA EDIADVVSRR TGIPVSQLTA SEKEKLLRLE EEMHSRIVGQ
DEAVTAVSQA VRRNRAGMGD PDRPVGSFLF LGPTGVGKTE LAKTLAELLF GDEDRMIRFD
MSEFQEKHTV ARLVGAPPGY VGYEEAGQLT EKVRRQPYSV VLFDEVEKAH PDVFNALLQL
LDDGRLTDAQ GRTVDFRHCV VIMTSNIGAQ RIIAHEGDVS EIKDELMEDL RGRFLPEFLN
RIDDIILFHS LTEEDLGEIV DHLLDQSEHR VHAQGIELDV TEAAKKLLIT HGHQPAFGAR
PLRRTIQTEL DNRLASLLLG GEAEHGDTIV ADVRDNSLHC TVSSDGAHPH GQDAAPKEEK
PARAKPVAEK DPKAPKAGKE APGTDPDAKS
//
