ID A0A0D6DXX3_9LACT Unreviewed; 758 AA.
AC A0A0D6DXX3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpE {ECO:0000313|EMBL:CEN28818.1};
GN Name=clpE {ECO:0000313|EMBL:CEN28818.1};
GN ORFNames=LACPI_1618 {ECO:0000313|EMBL:CEN28818.1};
OS Lactococcus piscium MKFS47.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=297352 {ECO:0000313|EMBL:CEN28818.1, ECO:0000313|Proteomes:UP000033166};
RN [1] {ECO:0000313|Proteomes:UP000033166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKFS47 {ECO:0000313|Proteomes:UP000033166};
RA Andreevskaya M.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; LN774769; CEN28818.1; -; Genomic_DNA.
DR RefSeq; WP_047915878.1; NZ_LN774769.1.
DR AlphaFoldDB; A0A0D6DXX3; -.
DR STRING; 1364.LP2241_50001; -.
DR KEGG; lpk:LACPI_1618; -.
DR HOGENOM; CLU_005070_4_3_9; -.
DR Proteomes; UP000033166; Chromosome I.
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; 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; 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:SF193; CHAPERONE PROTEIN CLPB; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 Hydrolase {ECO:0000313|EMBL:CEN28818.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CEN28818.1}.
FT DOMAIN 362..397
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 46..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 84105 MW; 5490B7361B0A598D CRC64;
MLCQNCQLNE ATIHLYTNMN GTKKQNDLCQ NCYQIMKAGG RENLLGGSAA NPSKNQSGND
FNPFDDLFGT LGNNASRANN RSDQSTPPTQ SGRAGNGNGG RGNSKAKGML EDFGFNVTES
ARKGEIDPVI GRDQEITRVI EILNRRTKNN PVLIGEPGVG KTAVVEGLAQ KIVDGDVPQK
LQNKEVIRLD VVSLVQGTGI RGQFEERMQK LMKEISSRKD VILFIDEIHE IVGAGAAGDG
NMDAGNILKP ALARGELQLV GATTLNEYRI IEKDAALERR MQPVKVDEPS VEETITILRG
IQSRYEDYHH VSYTDEAIEQ AAILSNRYIQ DRFLPDKAID LLDESGSKKN LTLKFIDPEE
IAKRIQSSEE AKNDALRSED FEKAAHFRDQ IAKLRELSKQ KLADEETPII TEKDIESIIE
EKTHIPVGDL KEKEQTQLIN LSDDLKGHVI GQDEAIDKIA KAVRRNRVGL GKANRPIGSF
MFVGPTGVGK TELAKQLALE LFGSQNSMIR FDMSEYMEKH SVAKLIGAPP GYVGYEEAGQ
LTEKVRRNPY SLILLDEIEK AHPDVMHMFL QILDDGRLTD AQGRTISFKD TIIIMTSNAG
TGKVEANVGF GAAREGLTNS VLGQLGDFFS PEFMNRFDAI IEFKTLSKEN LLKIVDLMLA
DVNGQIKRNE IHLEVTKEVK EKLVELGYDP KMGARPLRRT IQDHIEDKIA DFYIEHPDYK
NLLADLIDDE IVISSRVVAD QDDTTAIAST VSDDNETE
//
