ID A0A1I6T822_9BACI Unreviewed; 705 AA.
AC A0A1I6T822;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpE {ECO:0000313|EMBL:SFS85382.1};
GN ORFNames=SAMN05421668_11335 {ECO:0000313|EMBL:SFS85382.1};
OS Halolactibacillus miurensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halolactibacillus.
OX NCBI_TaxID=306541 {ECO:0000313|EMBL:SFS85382.1, ECO:0000313|Proteomes:UP000199139};
RN [1] {ECO:0000313|EMBL:SFS85382.1, ECO:0000313|Proteomes:UP000199139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17074 {ECO:0000313|EMBL:SFS85382.1,
RC ECO:0000313|Proteomes:UP000199139};
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; FPAI01000013; SFS85382.1; -; Genomic_DNA.
DR RefSeq; WP_062321110.1; NZ_FPAI01000013.1.
DR AlphaFoldDB; A0A1I6T822; -.
DR STRING; 306541.SAMN05421668_11335; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199139; 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 Hydrolase {ECO:0000313|EMBL:SFS85382.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFS85382.1}.
FT DOMAIN 331..366
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 705 AA; 79625 MW; 0C8EF8FAC9163DBD CRC64;
MKCQKCQVRP ANVNVTLRIN GHTEQLHVCD TCFKEIRNES LQPSNFFGQS GSAFEEQSGF
TKRQSHVKTE TPNHHDGLLD QLGRNLTDHA KQGLIDPVIG RDQEVTRVIE TLNRRNKNNP
VLIGEPGVGK TAIAEGLALK IAQGNVPKKL KDRQVYLLDV ASLVANTGVR GQFEERMKGL
ISELQDRQNV ILFVDEIHLL VGAGTAEGSQ MDAGNILKPA LARGELQLIG ATTLKEYRQI
EKDQALERRF QPIMVKEPTE QEAIQILQGI KERYESYHHV TYSDEVIEQA VRLSKRYIQD
RFLPDKAIDL IDEAGARLNL TLSESDQSTI EDELKYLAEE KQKAAEKEDY ETAAHLRHKE
LQLEKKLATH EGVPSIDVTT EAIQLLIEEK TGVPVRKMQA DDQQKMKDLK RHLEKKVIGQ
EVAVDKVAKA IRRSRAGLKS KHRPIGSFLF VGPTGVGKTE LTKVLAEEIF GHQDALIRLD
MSEYMEKHAV SKIIGSPPGY VGHEEAGQLT EKVRRQPYSV ILLDEIEKAH PDVQHMFLQI
MEDGRLTDSH GRVVNFKDTV IIMTSNAGSA VKELHVGFNK TETDAISTLD QLKDYFKPEF
LNRFDAIITF NQLEEEHLIK IVDLMLNELE ENLKEQGYRL EVTEKVKKHL ADIGYDRQFG
ARPLRRAIQE TLEDGITDVL LEEPDIMALK ADVIDDKIVV TKVSE
//