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   22-JUL-2008, entry version 69.
DE   RecName: Full=ATP-dependent hsl protease ATP-binding subunit hslU;
GN   Name=hslU; OrderedLocusNames=HI0497;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   MEDLINE=95350630; PubMed=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.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   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).
RX   MEDLINE=20560747; 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.,
RA   McKay D.B.;
RT   "Crystal and solution structures of an HslUV protease-chaperone
RT   complex.";
RL   Cell 103:633-643(2000).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   MEDLINE=20155479; PubMed=10693812; DOI=10.1038/35001629;
RA   Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D.,
RA   Huber R.;
RT   "The structures of HslU and the ATP-dependent protease HslU-HslV.";
RL   Nature 403:800-805(2000).
CC   -!- FUNCTION: Chaperone subunit of a proteasome-like degradation
CC       complex.
CC   -!- SUBUNIT: A double ring-shaped homohexamer of hslV is capped on
CC       each side by a ring-shaped hslU homohexamer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the clpX chaperone family. HslU subfamily.
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DR   EMBL; L42023; AAC22154.1; -; Genomic_DNA.
DR   RefSeq; NP_438655.1; -.
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=149-444.
DR   PDB; 1OFI; X-ray; 3.20 A; A/B/C=149-444.
DR   PDBsum; 1G3I; -.
DR   PDBsum; 1G41; -.
DR   PDBsum; 1IM2; -.
DR   PDBsum; 1KYI; -.
DR   PDBsum; 1OFH; -.
DR   PDBsum; 1OFI; -.
DR   DIP; DIP:6175N; -.
DR   IntAct; P43773; -.
DR   GeneID; 950614; -.
DR   GenomeReviews; L42023_GR; HI0497.
DR   KEGG; hin:HI0497; -.
DR   NMPDR; fig|71421.1.peg.468; -.
DR   TIGR; HI0497; -.
DR   HOGENOM; P43773; -.
DR   BioCyc; HINF71421:HI_0497-MON; -.
DR   LinkHub; P43773; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0009377; F:HslUV protease activity; IEA:HAMAP.
DR   HAMAP; MF_00249; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase_core.
DR   InterPro; IPR013093; ATPase_AAA-2.
DR   InterPro; IPR004491; HslU.
DR   PANTHER; PTHR11262:SF3; HslU; 1.
DR   Pfam; PF07724; AAA_2; 2.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR00390; hslU; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding.
FT   CHAIN         1    444       ATP-dependent hsl protease ATP-binding
FT                                subunit hslU.
FT                                /FTId=PRO_0000160508.
FT   NP_BIND      57     64       ATP.
FT   HELIX         6     14
FT   HELIX        21     39
FT   TURN         42     47
FT   STRAND       53     56
FT   HELIX        63     73
FT   STRAND       78     82
FT   HELIX        83     86
FT   HELIX        97    117
FT   HELIX       228    230
FT   HELIX       237    251
FT   STRAND      253    257
FT   HELIX       259    262
FT   STRAND      269    271
FT   HELIX       272    287
FT   STRAND      290    293
FT   STRAND      296    299
FT   STRAND      304    309
FT   HELIX       316    318
FT   HELIX       321    324
FT   STRAND      329    332
FT   HELIX       338    346
FT   HELIX       352    361
FT   TURN        362    364
FT   STRAND      366    369
FT   HELIX       371    387
FT   HELIX       392    394
FT   HELIX       395    410
FT   HELIX       411    413
FT   STRAND      418    421
FT   HELIX       423    430
FT   TURN        431    435
FT   HELIX       437    443
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
//