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Database: UniProt
Entry: A0A1H3YD43_9FIRM
LinkDB: A0A1H3YD43_9FIRM
Original site: A0A1H3YD43_9FIRM 
ID   A0A1H3YD43_9FIRM        Unreviewed;       483 AA.
AC   A0A1H3YD43;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=ATP-dependent HslUV protease ATP-binding subunit HslU {ECO:0000313|EMBL:SEA09527.1};
GN   ORFNames=SAMN04515656_103171 {ECO:0000313|EMBL:SEA09527.1};
OS   Eubacterium aggregans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=81409 {ECO:0000313|EMBL:SEA09527.1, ECO:0000313|Proteomes:UP000199394};
RN   [1] {ECO:0000313|EMBL:SEA09527.1, ECO:0000313|Proteomes:UP000199394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SR12 {ECO:0000313|EMBL:SEA09527.1,
RC   ECO:0000313|Proteomes:UP000199394};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000256|ARBA:ARBA00009771}.
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DR   EMBL; FNRK01000003; SEA09527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3YD43; -.
DR   STRING; 81409.SAMN04515656_103171; -.
DR   Proteomes; UP000199394; Unassembled WGS sequence.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
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   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004491; HslU.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00390; hslU; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:SEA09527.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:SEA09527.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:SEA09527.1};
KW   Protease {ECO:0000313|EMBL:SEA09527.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199394}.
FT   DOMAIN          54..376
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          375..469
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   483 AA;  54029 MW;  90D0299DA6016558 CRC64;
     MCAIEMKELT PKRIVSELNR YIIGQEKAKK AVAVSLRNRY RRSLLPEAER DEFTPKNIIL
     MGPTGVGKTE IARRIAKLVS APFIKVEATK FTEVGYVGRD VESMVRDLVT TSIRMVQQEK
     MKEVYEQAQA KAEGMILDVL VPQHKKQQKN ETLMNPFEIL SKMGNNTAAS NSQTTEVVPV
     EDPAKEAAIQ TKRAEIKKDL AAGKLEDEVI EIDVDDDGMK SIGMMAGMNE DMSISIGNIF
     DGLIPGGNKK KKKRTVKVSE ARKIITNQEA TKMIDMDEVH ELGLRAAEQS GIIFIDEIDK
     IIGNNGGNGP DVSREGVQRD ILPIVEGSTV TTKYGPVKTD FILFIGAGAF HVSKIEDMIP
     ELQGRFPVTV QLDSLTEEDF VQILTAPENA VVKQYTSLLR TEGVELHFDE AAIHKIAKIA
     FTKNEVEENI GARRLHTVFE ELLEEISFYA SDYDAEVFNI DEKYVESVFK LGDQERSYAK
     YFL
//
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