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Protein

Aminopeptidase S

Gene

SGR_5809

Organism
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149).3 Publications

Catalytic activityi

Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Calcium activates the enzyme, inhibited by 1,10-phenanthroline, EDTA and EGTA (PubMed:2503378). End-product inhibited by L-amino acids (PubMed:15388919). Non-competitively inhibited by NaF and NaH2PO4 (PubMed:17608735).4 Publications

Kineticsi

kcat is 390 s(-1) with Leu-pNA.1 Publication

  1. KM=0.59 mM for Leu-NH-Np (with zinc as cofactor)1 Publication
  2. KM=0.13 mM for Leu-NH-Np (with manganese as cofactor)1 Publication
  3. KM=0.046 mM for Leu-NH-Np (with cobalt as cofactor)1 Publication
  4. KM=4.1 mM for Ala-NH-Np (with zinc as cofactor)1 Publication
  5. KM=1.74 mM for Ala-NH-Np (with cobalt as cofactor)1 Publication
  6. KM=0.57 mM for Leu-pNA (with zinc as cofactor)1 Publication

    Temperature dependencei

    Stable after heating at 69 degrees Celsius for 5 hours.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi48 – 481Calcium2 Publications
    Metal bindingi49 – 491Calcium; via carbonyl oxygen2 Publications
    Metal bindingi130 – 1301Zinc 1; catalytic2 Publications
    Metal bindingi142 – 1421Zinc 1; catalytic2 Publications
    Metal bindingi142 – 1421Zinc 2; catalytic2 Publications
    Active sitei176 – 1761Proton acceptor2 Publications
    Metal bindingi177 – 1771Zinc 2; catalytic2 Publications
    Metal bindingi205 – 2051Zinc 1; catalytic2 Publications
    Sitei291 – 2911Transition state stabilizer2 Publications
    Metal bindingi292 – 2921Zinc 2; catalytic2 Publications
    Metal bindingi307 – 3071Calcium2 Publications
    Metal bindingi311 – 3111Calcium2 Publications

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciSGRI455632:GD3A-5884-MONOMER.
    BRENDAi3.4.11.24. 6035.
    SABIO-RKP80561.

    Protein family/group databases

    MEROPSiM28.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase S (EC:3.4.11.24)
    Alternative name(s):
    API1 Publication
    SGAP1 Publication
    Gene namesi
    Ordered Locus Names:SGR_5809
    OrganismiStreptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
    Taxonomic identifieri455632 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
    Proteomesi
    • UP000001685 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Biotechnological usei

    Sold by several companies as an extracellular extract called Pronase.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi176 – 1761E → A: KM halves (0.33 mM), kcat reduces by 5 orders of magnitude. 1 Publication
    Mutagenesisi176 – 1761E → D or Q: KM decreases (to 0.4 mM), kcat reduces by 4 orders of magnitude. 1 Publication
    Mutagenesisi291 – 2911Y → A, F or S: Activity decreases about 100-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 45452 PublicationsAdd
    BLAST
    Chaini46 – 329284Aminopeptidase SPRO_0000174143Add
    BLAST
    Propeptidei330 – 445116Removed in mature form1 PublicationPRO_0000431389Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi290 ↔ 2952 Publications

    Keywords - PTMi

    Disulfide bond, Zymogen

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi455632.SGR_5809.

    Structurei

    Secondary structure

    1
    445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi51 – 6616Combined sources
    Turni67 – 704Combined sources
    Helixi77 – 9317Combined sources
    Beta strandi96 – 1049Combined sources
    Beta strandi107 – 1159Combined sources
    Beta strandi119 – 13012Combined sources
    Turni140 – 1434Combined sources
    Helixi144 – 15916Combined sources
    Beta strandi165 – 17410Combined sources
    Helixi176 – 1783Combined sources
    Helixi181 – 1899Combined sources
    Helixi192 – 1954Combined sources
    Beta strandi198 – 2047Combined sources
    Beta strandi215 – 2173Combined sources
    Helixi221 – 23313Combined sources
    Beta strandi239 – 2413Combined sources
    Helixi250 – 2556Combined sources
    Beta strandi260 – 2645Combined sources
    Beta strandi268 – 2703Combined sources
    Helixi273 – 2797Combined sources
    Beta strandi285 – 2873Combined sources
    Turni289 – 2924Combined sources
    Helixi303 – 32119Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CP7X-ray1.58A46-329[»]
    1F2OX-ray1.70A46-329[»]
    1F2PX-ray1.80A46-329[»]
    1QQ9X-ray1.53A46-329[»]
    1TF8X-ray1.30A46-329[»]
    1TF9X-ray1.30A46-329[»]
    1TKFX-ray1.20A46-329[»]
    1TKHX-ray1.25A46-329[»]
    1TKJX-ray1.15A46-329[»]
    1XBUX-ray1.20A46-322[»]
    1XJOX-ray1.75A46-329[»]
    ProteinModelPortaliP80561.
    SMRiP80561. Positions 46-322.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80561.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M28 family. M28A subfamily.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105IIU. Bacteria.
    COG2234. LUCA.
    HOGENOMiHOG000268660.
    KOiK19702.
    OMAiVAFDRCY.
    OrthoDBiEOG68DCWW.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR008979. Galactose-bd-like.
    IPR007484. Peptidase_M28.
    IPR002884. PrprotnconvertsP.
    [Graphical view]
    PfamiPF01483. P_proprotein. 1 hit.
    PF04389. Peptidase_M28. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P80561-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRPNRFSLRR SPTAVAAVAL AAVLAAGAPA AQAAGAAAPT AAAAAAPDIP
    60 70 80 90 100
    LANVKAHLTQ LSTIAANNGG NRAHGRPGYK ASVDYVKAKL DAAGYTTTLQ
    110 120 130 140 150
    QFTSGGATGY NLIADWPGGD PNKVLMAGAH LDSVSSGAGI NDNGSGSAAV
    160 170 180 190 200
    LETALAVSRA GYQPDKHLRF AWWGAEELGL IGSKYYVNNL PSADRSKLAG
    210 220 230 240 250
    YLNFDMIGSP NPGYFVYDDD PVIEKTFKDY FAGLNVPTEI ETEGDGRSDH
    260 270 280 290 300
    APFKNVGVPV GGLFTGAGYT KSAAQAQKWG GTAGQAFDRC YHSSCDSLSN
    310 320 330 340 350
    INDTALDRNS DAAAHAIWTL SSGTGEPPTG EGVFSNTTDV AIPDAGAAVT
    360 370 380 390 400
    SSVAVTGRTG NAPAALQVGV DIKHTYRGDL VVDLLAPDGT AYRLKNSSSG
    410 420 430 440
    DSADNVIATY TVNASSEVAN GSWKLRVQDI ARQDTGYIDS WKLTF
    Length:445
    Mass (Da):45,940
    Last modified:November 26, 2014 - v2
    Checksum:i6B42B63191F700C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti185 – 1851Y → F AA sequence (PubMed:8665903).
    Sequence conflicti285 – 2851Q → R no nucleotide entry (PubMed:15280041).

    Mass spectrometryi

    Molecular mass is 29728±1.0 Da from positions 46 - 329. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AP009493 Genomic DNA. Translation: BAG22638.1.
    PIRiS66427.
    RefSeqiWP_012381549.1. NC_010572.1.

    Genome annotation databases

    EnsemblBacteriaiBAG22638; BAG22638; SGR_5809.
    GeneIDi6210128.
    KEGGisgr:SGR_5809.
    PATRICi23758425. VBIStrGri32265_5952.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AP009493 Genomic DNA. Translation: BAG22638.1.
    PIRiS66427.
    RefSeqiWP_012381549.1. NC_010572.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CP7X-ray1.58A46-329[»]
    1F2OX-ray1.70A46-329[»]
    1F2PX-ray1.80A46-329[»]
    1QQ9X-ray1.53A46-329[»]
    1TF8X-ray1.30A46-329[»]
    1TF9X-ray1.30A46-329[»]
    1TKFX-ray1.20A46-329[»]
    1TKHX-ray1.25A46-329[»]
    1TKJX-ray1.15A46-329[»]
    1XBUX-ray1.20A46-322[»]
    1XJOX-ray1.75A46-329[»]
    ProteinModelPortaliP80561.
    SMRiP80561. Positions 46-322.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi455632.SGR_5809.

    Protein family/group databases

    MEROPSiM28.003.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAG22638; BAG22638; SGR_5809.
    GeneIDi6210128.
    KEGGisgr:SGR_5809.
    PATRICi23758425. VBIStrGri32265_5952.

    Phylogenomic databases

    eggNOGiENOG4105IIU. Bacteria.
    COG2234. LUCA.
    HOGENOMiHOG000268660.
    KOiK19702.
    OMAiVAFDRCY.
    OrthoDBiEOG68DCWW.

    Enzyme and pathway databases

    BioCyciSGRI455632:GD3A-5884-MONOMER.
    BRENDAi3.4.11.24. 6035.
    SABIO-RKP80561.

    Miscellaneous databases

    EvolutionaryTraceiP80561.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR008979. Galactose-bd-like.
    IPR007484. Peptidase_M28.
    IPR002884. PrprotnconvertsP.
    [Graphical view]
    PfamiPF01483. P_proprotein. 1 hit.
    PF04389. Peptidase_M28. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Genome sequence of the streptomycin-producing microorganism Streptomyces griseus IFO 13350."
      Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., Yamashita A., Hattori M., Horinouchi S.
      J. Bacteriol. 190:4050-4060(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JCM 4626 / NBRC 13350.
    2. "Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases."
      Maras B., Greenblatt H.M., Shoham G., Spungin-Bialik A., Blumberg S., Barra D.
      Eur. J. Biochem. 236:843-846(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 46-329, FUNCTION, MASS SPECTROMETRY.
    3. "Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme."
      Spungin A., Blumberg S.
      Eur. J. Biochem. 183:471-477(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 46-51, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, THERMAL STABILITY.
    4. "Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution."
      Ben-Meir D., Spungin A., Ashkenazi R., Blumberg S.
      Eur. J. Biochem. 212:107-112(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus."
      Fundoiano-Hershcovitz Y., Rabinovitch L., Langut Y., Reiland V., Shoham G., Shoham Y.
      FEBS Lett. 571:192-196(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 115 AND 229, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, POSSIBLE REACTION MECHANISM, ACTIVE SITE, MUTAGENESIS OF GLU-176 AND TYR-291, EXPRESSION IN E.COLI.
      Strain: DSM 40855.
    6. "Catalytic mechanism of SGAP, a double-zinc aminopeptidase from Streptomyces griseus."
      Hershcovitz Y.F., Gilboa R., Reiland V., Shoham G., Shoham Y.
      FEBS J. 274:3864-3876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, REACTION MECHANISM, ACTIVE SITE.
    7. "Streptomyces griseus aminopeptidase: X-ray crystallographic structure at 1.75-A resolution."
      Greenblatt H.M., Almog O., Maras B., Spungin-Bialik A., Barra D., Blumberg S., Shoham G.
      J. Mol. Biol. 265:620-636(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ZINC, COFACTOR, SUBUNIT, DISULFIDE BOND.
    8. "Binding of inhibitory aromatic amino acids to Streptomyces griseus aminopeptidase."
      Reiland V., Gilboa R., Spungin-Bialik A., Schomburg D., Shoham Y., Blumberg S., Shoham G.
      Acta Crystallogr. D 60:1738-1746(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ZINC AND INHIBITORS, COFACTOR, ENZYME REGULATION, SUBUNIT, DISULFIDE BOND.

    Entry informationi

    Entry nameiAPX_STRGG
    AccessioniPrimary (citable) accession number: P80561
    Secondary accession number(s): B1W291
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: November 26, 2014
    Last modified: January 20, 2016
    This is version 95 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Most experiments use protein purified from a commercial source rather than protein that has been overexpressed.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.