(data stored in ACNUC7421 zone)

SWISSPROT: HSLV_SHESH

ID   HSLV_SHESH              Reviewed;         174 AA.
AC   A8FQM0;
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 subunit HslV {ECO:0000255|HAMAP-Rule:MF_00248};
DE            EC=3.4.25.2 {ECO:0000255|HAMAP-Rule:MF_00248};
GN   Name=hslV {ECO:0000255|HAMAP-Rule:MF_00248};
GN   OrderedLocusNames=Ssed_0531;
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: Protease subunit of a proteasome-like degradation
CC       complex believed to be a general protein degrading machinery.
CC       {ECO:0000255|HAMAP-Rule:MF_00248}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with
CC       broad specificity. {ECO:0000255|HAMAP-Rule:MF_00248}.
CC   -!- ENZYME REGULATION: Allosterically activated by HslU binding.
CC       {ECO:0000255|HAMAP-Rule:MF_00248}.
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_00248}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00248}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00248}.
DR   EMBL; CP000821; ABV35143.1; -; Genomic_DNA.
DR   RefSeq; WP_012140880.1; NC_009831.1.
DR   ProteinModelPortal; A8FQM0; -.
DR   SMR; A8FQM0; -.
DR   STRING; 425104.Ssed_0531; -.
DR   MEROPS; T01.006; -.
DR   EnsemblBacteria; ABV35143; ABV35143; Ssed_0531.
DR   KEGG; sse:Ssed_0531; -.
DR   eggNOG; ENOG4108R5P; Bacteria.
DR   eggNOG; COG5405; LUCA.
DR   HOGENOM; HOG000064533; -.
DR   KO; K01419; -.
DR   OMA; IMKGNAR; -.
DR   OrthoDB; POG091H024X; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR   GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:InterPro.
DR   CDD; cd01913; protease_HslV; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00248; HslV; 1.
DR   InterPro; IPR022281; ATP-dep_Prtase_HsIV_su.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR32194; PTHR32194; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PIRSF; PIRSF039093; HslV; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR03692; ATP_dep_HslV; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQM0.
DR   SWISS-2DPAGE; A8FQM0.
KW   Allosteric enzyme; Complete proteome; Cytoplasm; Hydrolase;
KW   Metal-binding; Protease; Sodium; Threonine protease.
FT   CHAIN         1    174       ATP-dependent protease subunit HslV.
FT                                /FTId=PRO_1000078431.
FT   ACT_SITE      2      2       {ECO:0000255|HAMAP-Rule:MF_00248}.
FT   METAL       157    157       Sodium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00248}.
FT   METAL       160    160       Sodium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00248}.
FT   METAL       163    163       Sodium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00248}.
SQ   SEQUENCE   174 AA;  18878 MW;  B3673318F43F314D CRC64;
     MTTIVSVRRN NQVVIAGDGQ VSLGNTVMKG NARKVRRLYH NKVLAGFAGG TADAFTLFER
     FEAKLEMHQG HLMKAAVEMA KDWRSDKMLR KLEALLAVAD DTCSLIITGN GDVVQPENDL
     ISIGSGGNFA QSAATALLEN TELSALEIAE KSLTIAGDIC VFTNQFKTIE ELNY
//

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