ID HSLU_HAEIN Reviewed; 444 AA.
AC P43773;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=ATP-dependent protease ATPase subunit HslU;
DE AltName: Full=Unfoldase HslU;
GN Name=hslU; OrderedLocusNames=HI_0497;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS) OF 2-175 IN COMPLEX WITH HSLV AND
RP ATP.
RX PubMed=11106733; DOI=10.1016/s0092-8674(00)00166-5;
RA Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., McKay D.B.;
RT "Crystal and solution structures of an HslUV protease-chaperone complex.";
RL Cell 103:633-643(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ADP AND SULFATE.
RX PubMed=11468391; DOI=10.1107/s0907444901007673;
RA Trame C.B., McKay D.B.;
RT "Structure of Haemophilus influenzae HslU protein in crystals with one-
RT dimensional disorder twinning.";
RL Acta Crystallogr. D 57:1079-1090(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLV;
RP MAGNESIUM; ADP AND INHIBITOR.
RX PubMed=12823960; DOI=10.1016/s0022-2836(03)00580-1;
RA Kwon A.-R., Kessler B.M., Overkleeft H.S., McKay D.B.;
RT "Structure and reactivity of an asymmetric complex between HslV and I-
RT domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome.";
RL J. Mol. Biol. 330:185-195(2003).
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.
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:0000269|PubMed:11106733,
CC ECO:0000269|PubMed:11468391, ECO:0000269|PubMed:12823960}.
CC -!- INTERACTION:
CC P43773; P43772: hslV; NbExp=4; IntAct=EBI-1030296, EBI-1030290;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22154.1; -; Genomic_DNA.
DR RefSeq; NP_438655.1; NC_000907.1.
DR PDB; 1G3I; X-ray; 3.41 A; A/B/C/D/E/F/S/T/U/V/W/X=1-444.
DR PDB; 1G41; X-ray; 2.30 A; A=1-444.
DR PDB; 1IM2; X-ray; 2.80 A; A=1-444.
DR PDB; 1KYI; X-ray; 3.10 A; A/B/C/D/E/F/S/T/U/V/W/X=1-444.
DR PDB; 1OFH; X-ray; 2.50 A; A/B/C=1-107, A/B/C=244-444.
DR PDB; 1OFI; X-ray; 3.20 A; A/B/C=1-107, A/B/C=244-444.
DR PDBsum; 1G3I; -.
DR PDBsum; 1G41; -.
DR PDBsum; 1IM2; -.
DR PDBsum; 1KYI; -.
DR PDBsum; 1OFH; -.
DR PDBsum; 1OFI; -.
DR AlphaFoldDB; P43773; -.
DR SMR; P43773; -.
DR DIP; DIP-6175N; -.
DR IntAct; P43773; 1.
DR STRING; 71421.HI_0497; -.
DR MEROPS; X20.005; -.
DR EnsemblBacteria; AAC22154; AAC22154; HI_0497.
DR KEGG; hin:HI_0497; -.
DR PATRIC; fig|71421.8.peg.515; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_6; -.
DR OrthoDB; 9804062at2; -.
DR PhylomeDB; P43773; -.
DR BioCyc; HINF71421:G1GJ1-510-MONOMER; -.
DR EvolutionaryTrace; P43773; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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 SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..444
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_0000160508"
FT REGION 143..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11106733"
FT BINDING 60..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11106733"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 306..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11106733"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 21..39
FT /evidence="ECO:0007829|PDB:1G41"
FT TURN 42..47
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1G3I"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1OFH"
FT HELIX 97..117
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1IM2"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1IM2"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 272..287
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1IM2"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1OFH"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:1G41"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 371..387
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 395..410
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:1G41"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 423..430
FT /evidence="ECO:0007829|PDB:1G41"
FT TURN 431..435
FT /evidence="ECO:0007829|PDB:1G41"
FT HELIX 437..443
FT /evidence="ECO:0007829|PDB:1G41"
SQ SEQUENCE 444 AA; 49372 MW; C346EA478E4094CE CRC64;
MSEMTPREIV SELDQHIIGQ ADAKRAVAIA LRNRWRRMQL QEPLRHEVTP KNILMIGPTG
VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDSAMKL VRQQEIAKNR
ARAEDVAEER ILDALLPPAK NQWGEVENHD SHSSTRQAFR KKLREGQLDD KEIEIDVSAG
VSMGVEIMAP PGMEEMTNQL QSLFQNLGSD KTKKRKMKIK DALKALIDDE AAKLINPEEL
KQKAIDAVEQ NGIVFIDEID KICKKGEYSG ADVSREGVQR DLLPLVEGST VSTKHGMVKT
DHILFIASGA FQVARPSDLI PELQGRLPIR VELTALSAAD FERILTEPHA SLTEQYKALM
ATEGVNIAFT TDAVKKIAEA AFRVNEKTEN IGARRLHTVM ERLMDKISFS ASDMNGQTVN
IDAAYVADAL GEVVENEDLS RFIL
//
