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Protein

Dipeptidyl aminopeptidase BI

Gene

dapb1

Organism
Pseudoxanthomonas mexicana
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sequentially removes dipeptide units (NH3-P2-P1-) from the amino termini of peptides and proteins. Is able to catalyze the removal of Asp-Arg from the amino termini of angiotensins I and II. Has slight endopeptidase activity on N-terminally blocked peptide derivatives which contain arginine residues at the P1 position. Does not hydrolyze Ala-Ala-Ala and Ala-Ala-Ala-Ala substrates or isulin beta chain.1 Publication

Enzyme regulationi

Nearly completely inhibited by 0.5 mM ZnCl2, 0.1 mM N-tosyl-L-lysyl chloromethyl ketone (TLCK) and 0.1 mM leupeptin. Strongly inhibited by 0.5 mM CoCl2 and 0.1 mM chymostatin. Activity is hardly affected by general serine protease inhibitors phenylmethanesulfonyl fluoride (PMSF), diisopropyl fluorophosphate (DFP) and N-tosyl-L-phenyl-alanyl chloromethyl ketone (TPCK) or by aspartyl protease inhibitor pepstatin A or by CaCl2 and EDTA. Cysteine protease inhibitors, such as N-ethylmaleimide (NEM), iodoacetic acid and L-trans-epoxysuccinyl-leucylamido(4-guanido)butane (E-64) have no effect on activity.2 Publications

Kineticsi

  1. KM=0.25 mM for Gly-Arg-pNA (at pH 9 and 37 degrees Celsius)1 Publication
  2. KM=0.019 mM for Arg-Arg-4-methoxy-beta-naphthylamide (Arg-Arg-MNA) (at pH 9 and 37 degrees Celsius)1 Publication
  3. KM=0.052 mM for Gly-Arg-MNA (at pH 9 and 37 degrees Celsius)1 Publication
  1. Vmax=195 µmol/min/mg enzyme with Gly-Arg-pNA as substrate (at pH 9 and 37 degrees Celsius)1 Publication
  2. Vmax=145 µmol/min/mg enzyme with Arg-Arg-MNA as substrate (at pH 9 and 37 degrees Celsius)1 Publication
  3. Vmax=95 µmol/min/mg enzyme with Gly-Arg-MNA as substrate (at pH 9 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 9.0 for the hydrolysis of Gly-Arg-pNA. No hydrolysis of Gly-Arg-pNA is detected below pH 5.5 or above pH 11.5. Stable over a broad pH range of between 7.5 and 10.0.1 Publication

Temperature dependencei

Optimum temperature is between 35 and 40 degrees Celsius for the hydrolysis of Gly-Arg-pNA. Stable for at least 30 minutes below 20 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei574 – 5741Charge relay systemPROSITE-ProRule annotationBy similarity
Active sitei659 – 6591Charge relay systemPROSITE-ProRule annotation
Active sitei694 – 6941Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • proteolysis involved in cellular protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Protein family/group databases

ESTHERipsesp-DAP. S9N_PREPL_Peptidase_S9.
MEROPSiS09.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl aminopeptidase BI1 PublicationImported (EC:3.4.14.-2 Publications)
Short name:
DAP BI2 Publications
Gene namesi
Name:dapb1Imported
OrganismiPseudoxanthomonas mexicana
Taxonomic identifieri128785 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaePseudoxanthomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 723700Dipeptidyl aminopeptidase BIPRO_0000433467Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO07834.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9A family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERiPTHR11757. PTHR11757. 1 hit.
PfamiPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSiPR00862. PROLIGOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O07834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPTSLLLAA TVLMSTPITS ALAASATPPD VAKKPHVVKA PHGAERNDEY
60 70 80 90 100
YWLRDDKREN KEMLAYLNAE NAYTDAVMAP LKPLEDKLYD EVVARIKQDD
110 120 130 140 150
ASVPYRERGW WYYARFVTGK DYPVHARRKD GPGVDAVSIQ AANAAGDFAG
160 170 180 190 200
EQVLLDVNAL GAGKDYYNVG DYEVSQDNRL LAYADDTNGR RQYTIRFKNL
210 220 230 240 250
DTGELLPDTV TNAEPNLVWS DDGRTLFYVD KDPETLLSKR VKAHVLGTPA
260 270 280 290 300
SQDALVYEEE DDSFYMGIGR SRDDKFICIS VESTVSSEMR CTPAASPGVF
310 320 330 340 350
TVLAPRERDV EYQADHLGDR WVIRTNADGA TNFKIVTAPT DSTSRKDWKD
360 370 380 390 400
WVAHRDDVFV EGFELFDGFS VVAERANALE SLRVIKADGS SDYVKADESA
410 420 430 440 450
YSMGLSANPE TGTDWLRYSY TSMTTPATTY EINTKTGERR QLKQQPVPGY
460 470 480 490 500
DASKYVTERV WAPARDGKTK IPVTLVYRKD VARDGKAPML QYAYGSYGAS
510 520 530 540 550
MDPNFSITNV SLLDRGVVYA LAHIRGGQEM GRAWYDDGKL YNKINTFTDF
560 570 580 590 600
IDVTDYLVKE GYAAKDRVAA MGGSAGGLLM GAVSNMAPEK YKVILTLVPF
610 620 630 640 650
VDVVTTMLDP TIPLTTNEYD EWGNPEEKGY YDYILTYSPY DNLQAKAYPA
660 670 680 690 700
MFVGTGLWDS QVQYWEPAKY VARLRDLNTG KGPVVFRTNM EAGHGGKSGR
710 720
FRQYRERAEM FAFMLDQLGV ASK
Length:723
Mass (Da):80,754
Last modified:July 1, 1997 - v1
Checksum:iD480FBC28FD78BC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004795 Genomic DNA. Translation: BAA20518.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004795 Genomic DNA. Translation: BAA20518.1.

3D structure databases

ProteinModelPortaliO07834.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERipsesp-DAP. S9N_PREPL_Peptidase_S9.
MEROPSiS09.010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERiPTHR11757. PTHR11757. 1 hit.
PfamiPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSiPR00862. PROLIGOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDAPB1_PSEMX
AccessioniPrimary (citable) accession number: O07834
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2015
Last sequence update: July 1, 1997
Last modified: November 11, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.