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HSLU_HAEIN
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   03-AUG-2022, entry version 150.
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; Proteobacteria; 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   RefSeq; WP_010868991.1; 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   OMA; KYGMIKT; -.
DR   PhylomeDB; P43773; -.
DR   BioCyc; HINF71421:G1GJ1-510-MON; -.
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   Gene3D; 3.40.50.300; -; 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   PANTHER; PTHR48102:SF3; PTHR48102:SF3; 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; SSF52540; 1.
DR   TIGRFAMs; TIGR00390; hslU; 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
 
 
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