ID S2YLY4_9BACL Unreviewed; 464 AA.
AC S2YLY4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000256|HAMAP-Rule:MF_00249};
DE AltName: Full=Unfoldase HslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN Name=hslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN ORFNames=HMPREF1210_01104 {ECO:0000313|EMBL:EPD52724.1};
OS Paenisporosarcina sp. HGH0030.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae;
OC Paenisporosarcina.
OX NCBI_TaxID=1078085 {ECO:0000313|EMBL:EPD52724.1, ECO:0000313|Proteomes:UP000014412};
RN [1] {ECO:0000313|EMBL:EPD52724.1, ECO:0000313|Proteomes:UP000014412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGH0030 {ECO:0000313|EMBL:EPD52724.1,
RC ECO:0000313|Proteomes:UP000014412};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Paenisporosarcina sp. HGH0030.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; this
CC subunit has chaperone activity. The binding of ATP and its subsequent
CC hydrolysis by HslU are essential for unfolding of protein substrates
CC subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of
CC its protein substrates and unfolds these before they are guided to HslV
CC for hydrolysis. {ECO:0000256|HAMAP-Rule:MF_00249}.
CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on each
CC side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV
CC complex is dependent on binding of ATP. {ECO:0000256|HAMAP-
CC Rule:MF_00249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000256|ARBA:ARBA00009771, ECO:0000256|HAMAP-Rule:MF_00249}.
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:EPD52724.1}.
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DR EMBL; AGEQ01000006; EPD52724.1; -; Genomic_DNA.
DR RefSeq; WP_016427614.1; NZ_KE150421.1.
DR AlphaFoldDB; S2YLY4; -.
DR STRING; 1078085.HMPREF1210_01104; -.
DR PATRIC; fig|1078085.3.peg.1085; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_9; -.
DR Proteomes; UP000014412; Unassembled WGS sequence.
DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19498; RecA-like_HslU; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00249; HslU; 1.
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 Pfam; PF10431; ClpB_D2-small; 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:0000256|HAMAP-Rule:MF_00249};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00249};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249};
KW Hydrolase {ECO:0000313|EMBL:EPD52724.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:EPD52724.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014412}.
FT DOMAIN 51..357
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 356..455
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT BINDING 20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 62..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 464 AA; 52177 MW; 973DF06EA18C0300 CRC64;
MIKQQLTPKQ ITEHLDRFIV GQKEAKKSVA VALRNRYRRS LLSDEMKNEV IPKNILMIGP
TGVGKTEIAR RIAKLTNAPF IKVEATKFTE VGYVGRDVES MVRDLTEAAV RIVKEEMTEG
VKAQAERLAN DAIVRLLVPS LKKKHNTQNP FEMLFGQKAE QEEPANDDTD IRLKRSQIAE
DLRDGKLEDE WVNVEVTEQA PSMFDAFQGS GMESMGQNMQ DALSNLMPKK KKKRRLQVKD
ARRVLTLEEA HKLIDSEEVA QKSIERAEQT GIIFIDEIDK IASKGGNGSS ADVSREGVQR
DILPIVEGST VQTKYGAVKT DYMLFVAAGA FHTAKPSDLI PELQGRFPVR VELEKLSKDD
FVRILKEPDH SLIRQYKSLL ETEGVTLEFT DSAIERIAEI ATEVNQESDN IGARRLHTIL
EKLLEELSYE ASDIAPAHID ITPAYVDQKL GNIVKNKDLS QFIL
//