ID A0A369B7T2_9ENTE Unreviewed; 465 AA.
AC A0A369B7T2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ECO:0000313|EMBL:NKC67878.1};
GN ORFNames=CBF32_03105 {ECO:0000313|EMBL:RSU04380.1}, HED35_07250
GN {ECO:0000313|EMBL:NKC67878.1}, JZO80_02585
GN {ECO:0000313|EMBL:MBO0419035.1};
OS Vagococcus fluvialis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=2738 {ECO:0000313|EMBL:NKC67878.1, ECO:0000313|Proteomes:UP000521358};
RN [1] {ECO:0000313|EMBL:RSU04380.1, ECO:0000313|Proteomes:UP000288197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCFB 2497 {ECO:0000313|EMBL:RSU04380.1,
RC ECO:0000313|Proteomes:UP000288197};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NKC67878.1, ECO:0000313|Proteomes:UP000521358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFMG-H7 {ECO:0000313|EMBL:NKC67878.1,
RC ECO:0000313|Proteomes:UP000521358};
RA Giannattasio-Ferraz S., Maskeri L., Penido A., Barbosa-Stancioli E.F.,
RA Putonti C.;
RT "Bacterial samples isolated from urine from healthy bovine heifers (Gyr
RT breed).";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MBO0419035.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DIV0015 {ECO:0000313|EMBL:MBO0419035.1};
RA Gilmore M.S., Schwartzman J., Van Tyne D., Martin M., Earl A.M.,
RA Manson A.L., Straub T., Salamzade R., Saavedra J., Lebreton F.,
RA Prichula J., Schaufler K., Gaca A., Sgardioli B., Wagenaar J., Strong T.;
RT "Enterococcal diversity collection.";
RL Submitted (MAR-2021) 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:NKC67878.1}.
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DR EMBL; JAFLWJ010000002; MBO0419035.1; -; Genomic_DNA.
DR EMBL; JAAVMB010000007; NKC67878.1; -; Genomic_DNA.
DR EMBL; NGJX01000002; RSU04380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369B7T2; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000288197; Unassembled WGS sequence.
DR Proteomes; UP000521358; Unassembled WGS sequence.
DR Proteomes; UP000664375; 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; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249};
KW Hydrolase {ECO:0000313|EMBL:NKC67878.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:NKC67878.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288197}.
FT DOMAIN 51..358
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 357..456
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 152..179
FT /evidence="ECO:0000256|SAM:Coils"
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 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 465 AA; 52537 MW; 54DAA37C2BBBED8F CRC64;
MTTNQKTPRE IVSELDKYII GQQTAKKSVS VALRNRYRRM QLDEDMQQEI TPKNLLMIGP
TGVGKTEIAR RLAKIVNAPF VKVEATKFTE VGYVGRDVES MVRDLVEASI GIVKKEQYSR
VYSQALKKAE DRLVKLLVPG IKKEKKQQTS QLDMMMQMMN GLQNNQEEEK EEINDSIRVS
RETVQSQLEK GLLENREITI EVEEKKSAPS MNNGLEQMGI DLSDTLNSLT PKKKVKRTVT
VAEAREILVN EESEKLVNDA DIHSEAISLA QNHGIIFIDE FDKITSKSEN SGQVSREGVQ
RDILPIVEGS LVNTKYGTVS TEHILFIASG AFHLSKPSDL IPELQGRFPI RVELDDLTAE
DFVKILTEPD NALVKQYIAL LGTENISVTF TKEAIEKIAE IAFEVNSETD NIGARRLHTI
LEKLLEDLLF ESPDMQMGEI TITESYVNEK LDHIVKDEDL SRYIL
//