DAPB3_PSEMX
ID DAPB3_PSEMX Reviewed; 689 AA.
AC V5YMB3;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Dipeptidyl aminopeptidase BIII {ECO:0000312|EMBL:BAO18428.1};
DE Short=DAP BIII {ECO:0000303|PubMed:8892831};
DE EC=3.4.14.- {ECO:0000269|PubMed:8892831};
DE Flags: Precursor;
GN Name=dapb3 {ECO:0000312|EMBL:BAO18428.1};
OS Pseudoxanthomonas mexicana.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=128785;
RN [1] {ECO:0000312|EMBL:BAO18428.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO24 {ECO:0000312|EMBL:BAO18428.1};
RA Suzuki Y., Ogasawara W.;
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=WO24 {ECO:0000303|PubMed:8892831};
RX PubMed=8892831; DOI=10.1128/jb.178.21.6288-6295.1996;
RA Ogasawara W., Kobayashi G., Okada H., Morikawa Y.;
RT "Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain
RT WO24.";
RL J. Bacteriol. 178:6288-6295(1996).
CC -!- FUNCTION: Exopeptidase that catalyzes the removal of dipeptide units
CC (NH2-P2-P1- or -P1'-P2'-COOH) from the free amino or carboxy termini.
CC Prefers substrates composed of bulky, hydrophobic amino acids at P1 and
CC P1' positions. Has endopeptidase activity on N-terminally blocked
CC peptide derivatives which contain aromatic amino acid residue at the P1
CC position. Exopeptidase activity is much higher than its endopeptidase
CC activity. {ECO:0000269|PubMed:8892831}.
CC -!- ACTIVITY REGULATION: Strongly inhibited by the serine protease
CC inhibitor diisopropyl fluorophosphate (DFP), chymostatin, leupeptin,
CC 0.5 mM ZnCl(2), 10 mM o-phenanthlorine and N-tosyl-L-phenyl-alanyl
CC chloromethyl ketone (TPCK), but not by N-tosyl-L-lysyl chloromethyl
CC ketone (TLCK). Activity is not affected significantly by iodoacetate
CC (IAA), L-trans-epoxysuccinyl-leucylamido(4-guanido)butane (E64),
CC pepstatin A and phenylmethanesulfonyl fluoride (PMSF). Activity is
CC stimulated by addition of 0.5 mM CaCl(2), 10 mM EDTA and N-
CC ethylmaleimide (NEM). {ECO:0000269|PubMed:8892831}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 mM for Gly-Phe-pNA (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8892831};
CC KM=1.0 mM for Gly-Phe-beta-naphthylamine (at pH 9 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:8892831};
CC Vmax=9.6 umol/min/mg enzyme with Gly-Phe-pNA as substrate (at pH 9
CC and 37 degrees Celsius) {ECO:0000269|PubMed:8892831};
CC Vmax=330 umol/min/mg enzyme with Gly-Phe-beta-naphthylamine as
CC substrate (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8892831};
CC pH dependence:
CC Optimum pH is 8.5 to 9.0 for the hydrolysis of Gly-Phe-pNA.
CC {ECO:0000269|PubMed:8892831};
CC Temperature dependence:
CC Optimum temperature is between 35 and 40 degrees Celsius for the
CC hydrolysis of Gly-Phe-pNA. Stable at a temperature below 20 degrees
CC Celsius for 30 minutes. {ECO:0000269|PubMed:8892831};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8892831}.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR EMBL; AB889526; BAO18428.1; -; Genomic_DNA.
DR AlphaFoldDB; V5YMB3; -.
DR SMR; V5YMB3; -.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Hydrolase; Protease; Serine protease; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..689
FT /note="Dipeptidyl aminopeptidase BIII"
FT /id="PRO_0000433468"
FT ACT_SITE 506
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P13798,
FT ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 593
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 625
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P13798,
FT ECO:0000255|PROSITE-ProRule:PRU10084"
SQ SEQUENCE 689 AA; 74228 MW; 330AC6C85C326406 CRC64;
MRHPAFRLTL LASTVAFALA PQAAQAAPSA ADRIAGTELI ARDALFGNPE RANVQISPDG
KYLSWVAAVD GVLNVWIAPA DNPSQARAVT QDTARGIRSY FWSYQPDTLL YLRDSGGDED
FHLYAVDLKT GQAKDLTPFP KTTAQVAGVS PKHPGTILVG MNDRDAQWHD IYKVDLASGN
RTLLEKNDAQ IAGYIADADY TLKYAQRSRP DGGADVLRRG ANGAWEKFDD IPFEDVLTTS
PGGLTLDGKT LYFTDSRGRN TAALFAIDVA SGKRTLVLED ARADVGGTLA DPATGKVQAV
SVDYLRDEWK VVDPAIRADL EKLEAIGPGD VSVNTRTLDD KTWIVAYSAA EAPLVYYRYD
RSAGTLTKLF SARPKLEGKP LVPQWPVEIA SRDNKTLVSY LTLPRSADAN NDGKADAPVP
LVLLVHGGPW ARDSYGYGGY NQWLANRGYA VLSVNFRGST GFGKDFTNAG NGEWAGKMHD
DLIDAVQWAV KQGVTTQDQV AIMGGSYGGY ATLTGLTFTP DAFACGVDIV GPSNLNTLLS
TVPPYWASFF EQLAKRMGDP RTDAGKKWLT ERSPLTRADQ IKKPLLIGQG ANDPRVKQAE
SDQIVKAMQA KNIPVTYVLF PDEGHGFARP ENNKAFNAVT EGFLAQCLGG RAEPIGKDFT
GSSISVPVGA DGVPGLAEAL KGHTQEVKK
