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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Metal bindingi48Calcium2 Publications1
    Metal bindingi49Calcium; via carbonyl oxygen2 Publications1
    Metal bindingi130Zinc 1; catalytic2 Publications1
    Metal bindingi142Zinc 1; catalytic2 Publications1
    Metal bindingi142Zinc 2; catalytic2 Publications1
    Active sitei176Proton acceptor2 Publications1
    Metal bindingi177Zinc 2; catalytic2 Publications1
    Metal bindingi205Zinc 1; catalytic2 Publications1
    Sitei291Transition state stabilizer2 Publications1
    Metal bindingi292Zinc 2; catalytic2 Publications1
    Metal bindingi307Calcium2 Publications1
    Metal bindingi311Calcium2 Publications1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi176E → A: KM halves (0.33 mM), kcat reduces by 5 orders of magnitude. 1 Publication1
    Mutagenesisi176E → D or Q: KM decreases (to 0.4 mM), kcat reduces by 4 orders of magnitude. 1 Publication1
    Mutagenesisi291Y → A, F or S: Activity decreases about 100-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 452 PublicationsAdd BLAST45
    ChainiPRO_000017414346 – 329Aminopeptidase SAdd BLAST284
    PropeptideiPRO_0000431389330 – 445Removed in mature form1 PublicationAdd BLAST116

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    1445
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi51 – 66Combined sources16
    Turni67 – 70Combined sources4
    Helixi77 – 93Combined sources17
    Beta strandi96 – 104Combined sources9
    Beta strandi107 – 115Combined sources9
    Beta strandi119 – 130Combined sources12
    Turni140 – 143Combined sources4
    Helixi144 – 159Combined sources16
    Beta strandi165 – 174Combined sources10
    Helixi176 – 178Combined sources3
    Helixi181 – 189Combined sources9
    Helixi192 – 195Combined sources4
    Beta strandi198 – 204Combined sources7
    Beta strandi215 – 217Combined sources3
    Helixi221 – 233Combined sources13
    Beta strandi239 – 241Combined sources3
    Helixi250 – 255Combined sources6
    Beta strandi260 – 264Combined sources5
    Beta strandi268 – 270Combined sources3
    Helixi273 – 279Combined sources7
    Beta strandi285 – 287Combined sources3
    Turni289 – 292Combined sources4
    Helixi303 – 321Combined sources19

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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.

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti185Y → F AA sequence (PubMed:8665903).1
    Sequence conflicti285Q → R no nucleotide entry (PubMed:15280041).1

    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
    PDB 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.
    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.

    Enzyme and pathway databases

    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...

    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: November 2, 2016
    This is version 98 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.