ID A0A1I0YTA3_9BACI Unreviewed; 709 AA.
AC A0A1I0YTA3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpE {ECO:0000313|EMBL:SFB16619.1};
GN ORFNames=SAMN04488072_108169 {ECO:0000313|EMBL:SFB16619.1};
OS Lentibacillus halodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=237679 {ECO:0000313|EMBL:SFB16619.1, ECO:0000313|Proteomes:UP000198642};
RN [1] {ECO:0000313|EMBL:SFB16619.1, ECO:0000313|Proteomes:UP000198642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3702 {ECO:0000313|EMBL:SFB16619.1,
RC ECO:0000313|Proteomes:UP000198642};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOJW01000008; SFB16619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0YTA3; -.
DR STRING; 237679.SAMN04488072_108169; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198642; Unassembled WGS sequence.
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:SF175; ATP-DEPENDENT CLP PROTEASE, ATP-BINDING SUBUNIT CLPC; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:SFB16619.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFB16619.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198642}.
FT DOMAIN 335..370
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 324..377
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 709 AA; 79563 MW; 96DDE7E721031FDC CRC64;
MQCQNCGIRP AAINVSMQIN NERMNMHLCN ECFQEIQNSM MNGDFGQGQQ GDFANKFFQG
NGQNQGFTGT KTQQGSGNGN GLLDQMGKNV TNAARAGLID PVIGRDNEVK RVIETLNRRN
KNNPVLIGEP GVGKTAIAEG LALKITEGKV PAKLMDKEIY LLDVASLVAN TSMRGQFEER
MKQLVQELQE RQNVILFVDE IHLLVGAGTA ESSQMDAGNI LKPALARGEL QLIGATTLKE
YRQIEKDAAL ERRFQPVMVK EPSVEDAVQI LQGIKDRYEK FHEVKYSDEA IRAFVTLSQR
YIQDRFLPDK AIDLMDEVGS RLNLDNAEKD SDSIQNRLDE VVREKEAAAE KEDYETAAHL
RYQEIQLQKQ LEKAKDEEQV VDVDISDIQL IVEEKTGIPV TKLQRDEQEK MRNLGEYLSA
KVIGQEEAVQ KVAKAVRRSR AGLKSKYRPI GSFLFVGPTG VGKTELTKAL AEELFGSRDS
LIRLDMSEYM EKHAVSKIIG SPPGYVGHEE AGQLTEKVRR NPYNIILLDE IEKAHPDVQN
TFLQIMEDGQ LTDSHGRTVS FKDTVMIMTS NAGTGEKQIN VGFNRDEHDA VSTLENLSAY
FKPEFLNRFD SIIQFNELQE ESLLQIVDLM LGELEKTIEE NAISISITDA AKHELVQLGY
DRRFGARPLR RVIQDKIEDQ LTDLILEEET VDTVQVDVKD GEIVVGKSE
//