ID A0A117PEX4_9ACTN Unreviewed; 849 AA.
AC A0A117PEX4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=AAA family ATPase {ECO:0000313|EMBL:KUM78400.1};
GN ORFNames=AQI70_13070 {ECO:0000313|EMBL:KUM78400.1};
OS Streptomyces curacoi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146536 {ECO:0000313|EMBL:KUM78400.1, ECO:0000313|Proteomes:UP000054024};
RN [1] {ECO:0000313|EMBL:KUM78400.1, ECO:0000313|Proteomes:UP000054024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40107 {ECO:0000313|EMBL:KUM78400.1,
RC ECO:0000313|Proteomes:UP000054024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces curacoi DSM 40107, type strain for
RT the species Streptomyces curacoi.";
RL Submitted (OCT-2015) 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:KUM78400.1}.
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DR EMBL; LMWJ01000007; KUM78400.1; -; Genomic_DNA.
DR RefSeq; WP_062147958.1; NZ_KQ947986.1.
DR AlphaFoldDB; A0A117PEX4; -.
DR STRING; 146536.AQI70_13070; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000054024; 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 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, ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000054024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 34..182
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 452..487
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 78..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..494
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 849 AA; 93115 MW; 3D64BFD02B2716A0 CRC64;
MTSGFSGPED YDPFGEFLAR FFGGPRPGPR QIDIGRLLSQ PARELVRGAA QYAAEHGSRD
LDTQHLLRAA LAAEPTRSLL SRAGADPDSL ATEIDERSGP VQHPPGEAPP PTSLSLTPAA
KRALLDAHDL ARSRGAGYIG PEHVLSALAA NPDSAAGHIL NAARFAPSGP PEAPEAAPSR
PHVDQRPRVD TGTPTLDKYG RDLTDLARRG GIDPVIGREE EIEQTIEVLS RRGKNNPVLI
GDAGVGKTAI VEGLAQRIAE SDVPDVLSGR RVIALDLTGV VAGTRYRGDF EERLNNIVGE
IRSHSDQLIV FIDELHTVVG AGGGGEGGSM DAGNILKPAL ARGELHIVGA TTLEEYRRIE
KDAALSRRFQ PIMVPEPTPS DAIEILRGLR DRYEAHHQVR YTDEALVAAV ELSDRYLTDR
RLPDKAIDLI DQAGARVRLR ARTKGTDVRA MEREVEQLYR DKDQAVADEQ YEQATQLRDH
IVELKQRIAD ASGDEEADEG QHLEVTAEAI AEVVSRQTGI PVSSLTEEEK DRLLGLEEHL
HERVVGQDEA VRVVSDAVLR SRAGLASPDR PIGSFFFLGP TGVGKTELAR ALAEALFGSE
ERMVRLDMSE YQERHTVSRL IGAPPGYVGH EEAGQLTEVV RRHPYSLLLL DEVEKAHPDV
FNILLQVLDD GRLTDSQGRT VDFTNTVIVM TSNLGSEAIT RGGTGIGFGA GDAEADEEAR
RERILRPLRE HFRPEFLNRI DEVVVFRQLT HDQLERITNL LLEQTRRLLR AQGVSVDFTD
SAVDWLSERG YQPEYGARPL RRTIQKEVDN QLSRLLLDGR IGEGGRVTVD VEDGRLAFRT
EELPPAPEL
//