(data stored in ACNUC7421 zone)

SWISSPROT: HSLU_PSEU2

ID   HSLU_PSEU2              Reviewed;         445 AA.
AC   Q4ZZF8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000255|HAMAP-Rule:MF_00249};
DE   AltName: Full=Unfoldase HslU {ECO:0000255|HAMAP-Rule:MF_00249};
GN   Name=hslU {ECO:0000255|HAMAP-Rule:MF_00249};
GN   OrderedLocusNames=Psyr_0394;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex;
CC       this subunit has chaperone activity. The binding of ATP and its
CC       subsequent hydrolysis by HslU are essential for unfolding of
CC       protein substrates subsequently hydrolyzed by HslV. HslU
CC       recognizes the N-terminal part of its protein substrates and
CC       unfolds these before they are guided to HslV for hydrolysis.
CC       {ECO:0000255|HAMAP-Rule:MF_00249}.
CC   -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on
CC       each side by a ring-shaped HslU homohexamer. The assembly of the
CC       HslU/HslV complex is dependent on binding of ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_00249}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00249}.
DR   EMBL; CP000075; AAY35464.1; -; Genomic_DNA.
DR   RefSeq; WP_003316641.1; NC_007005.1.
DR   RefSeq; YP_233502.1; NC_007005.1.
DR   SMR; Q4ZZF8; -.
DR   STRING; 205918.Psyr_0394; -.
DR   EnsemblBacteria; AAY35464; AAY35464; Psyr_0394.
DR   GeneID; 3365870; -.
DR   KEGG; psb:Psyr_0394; -.
DR   PATRIC; fig|205918.7.peg.408; -.
DR   eggNOG; ENOG4105C4N; Bacteria.
DR   eggNOG; COG1220; LUCA.
DR   HOGENOM; HOG000010036; -.
DR   KO; K03667; -.
DR   OMA; KYGMIKT; -.
DR   BioCyc; PSYR205918:G1G4J-395-MONOMER; -.
DR   Proteomes; UP000000426; Chromosome.
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:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
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; PTHR43815; PTHR43815; 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; SSF52540; 1.
DR   TIGRFAMs; TIGR00390; hslU; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4ZZF8.
DR   SWISS-2DPAGE; Q4ZZF8.
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Stress response.
FT   CHAIN         1    445       ATP-dependent protease ATPase subunit
FT                                HslU.
FT                                /FTId=PRO_1000012779.
FT   NP_BIND      59     64       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
FT   BINDING      17     17       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00249}.
FT   BINDING     254    254       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
FT   BINDING     319    319       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
FT   BINDING     391    391       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
SQ   SEQUENCE   445 AA;  49896 MW;  719CB935CC0F9BD5 CRC64;
     MSMTPREIVH ELNRHIIGQD DAKRAVAIAL RNRWRRMQLP EELRVEVTPK NILMIGPTGV
     GKTEIARRLA KLANAPFIKV EATKFTEVGY VGRDVESIIR DLADAAIKLL REQEIVKVRH
     RAEDAAEERI LDALLPPARV GFNEDPAQSS DSNTRQLFRK RLREGQLDDK EIEIEINEAV
     GVDISAPPGM EEMTNQLQSL FANMGKGKTK SRKLKVKEAL KLVREEEAGR LVNEEELKAK
     ALEAVEQHGI VFIDEIDKVA KRGNSGGVDV SREGVQRDLL PLIEGCTVNT KLGMVKTDHI
     LFIASGAFHL SKPSDLVPEL QGRLPIRVEL KALSPQDFER ILSEPHASLT EQYRELLKTE
     GLKIEFKPEG IKRLAEIAWQ VNEKTENIGA RRLHTLLERL LEEVSFSAGD LAISPDAAPI
     EIDAEYVNSH LGDLAENEDL SRYIL
//

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