(data stored in ACNUC7421 zone)

SWISSPROT: HSLU_SHESH

ID   HSLU_SHESH              Reviewed;         441 AA.
AC   A8FQL9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 70.
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=Ssed_0530;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000821; ABV35142.1; -; Genomic_DNA.
DR   RefSeq; WP_012140879.1; NC_009831.1.
DR   ProteinModelPortal; A8FQL9; -.
DR   STRING; 425104.Ssed_0530; -.
DR   PRIDE; A8FQL9; -.
DR   EnsemblBacteria; ABV35142; ABV35142; Ssed_0530.
DR   KEGG; sse:Ssed_0530; -.
DR   eggNOG; ENOG4105C4N; Bacteria.
DR   eggNOG; COG1220; LUCA.
DR   HOGENOM; HOG000010036; -.
DR   KO; K03667; -.
DR   OMA; KYGMIKT; -.
DR   OrthoDB; POG091H01U4; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro.
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   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   3: Inferred from homology;
DR   PRODOM; A8FQL9.
DR   SWISS-2DPAGE; A8FQL9.
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Stress response.
FT   CHAIN         1    441       ATP-dependent protease ATPase subunit
FT                                HslU.
FT                                /FTId=PRO_1000078457.
FT   NP_BIND      60     65       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
FT   BINDING      18     18       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   441 AA;  50053 MW;  4F2F06B985E9975E CRC64;
     MSEMTPREIV HELDTHIIGQ HDAKRSVAIA LRNRWRRMQL DVDFRQEVTP KNILMIGPTG
     VGKTEIARRL AKLAKAPFIK VEATKFTEVG YVGKEVEQII RDLTDSAIKM TREDQMKKCK
     FKAEEAAEER ILDALLPKPK EDWDNEKPDD SATRQIFRKK LREGQLDDKE IEIDVAAPQV
     GIEIMSPPGM EEMTNQLQSM FQNMGPGDSK RRKMPIKEAY KLMIEEEAAK LVNQDDMKEQ
     AIELVEQHGI VFLDEIDKIC KRGESSGPDV SREGVQRDLL PLVEGCTVNT KHGMVKTDHI
     LFIASGAFQM SKPSDLIPEL QGRLPIRVEL SALTADDFKR ILTEPHASLT EQHVAMMGTE
     DVKIEFTEDG IESIAQAAWQ VNERTENIGA RRLHTVMERL MEDLSYDASD KSGNTFVIDA
     EYVSSHLDDL VQDEDLSRFI L
//

If you have problems or comments...

PBIL Back to PBIL home page