(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Xanthomonadales: NE > Xanthomonadaceae: NE > Stenotrophomonas: NE > Stenotrophomonas maltophilia group: NE > Stenotrophomonas maltophilia: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Stenotrophomonas maltophilia: N, E.
Stenotrophomonas maltophilia R551-3: N, E.
Stenotrophomonas maltophilia SKK35: N, E.
Stenotrophomonas maltophilia MF89: N, E.
Stenotrophomonas maltophilia 5BA-I-2: N, E.
Stenotrophomonas maltophilia M30: N, E.
Stenotrophomonas maltophilia JV3: N, E.
Stenotrophomonas maltophilia RA8: N, E.
Stenotrophomonas maltophilia K279a: N, E.
Stenotrophomonas maltophilia Ab55555: N, E.
Stenotrophomonas maltophilia EPM1: N, E.
Stenotrophomonas maltophilia D457: N, E.
Stenotrophomonas maltophilia AU12-09: N, E.
Molecular evidence
Database
No mutation 1 structure: 2ECF: Crystal Structure of Dipeptidyl Aminopeptidase IV from Stenotrophomonas maltophilia No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MRHLFASLAFMLATSTVAHAEKLTLEAITGPLPLSGPTLMKPKVAPDGSR VTFLRGKDSDRNQLDLWSYDIGSGQTRLLVDSKVVLPGTETLSDEEKARR ERQRIAAMTGIVDYQWSPDAQRLLFPLGGELYLYDLKQEGKAAVRQLTHG EGFATDAKLSPKGGFVSFIRGRNLWVIDLASGRQMQLTADGSTTIGNGIA EFVADEEMDRHTGYWWAPDDSAIAYARIDESPVPVQKRYEVYADRTDVIE QRYPAAGDANVQVKLGVISPAEQAQTQWIDLGKEQDIYLARVNWRDPQHL SFQRQSRDQKKLDLVEVTLASNQQRVLAHETSPTWVPLHNSLRFLDDGSI LWSSERTGFQHLYRIDSKGKAAALTHGNWSVDELLAVDEKAGLAYFRAGI ESARESQIYAVPLQGGQPQRLSKAPGMHSASFARNASVYVDSWSNNSTPP QIELFRANGEKIATLVENDLADPKHPYARYREAQRPVEFGTLTAADGKTP LNYSVIKPAGFDPAKRYPVAVYVYGGPASQTVTDSWPGRGDHLFNQYLAQ QGYVVFSLDNRGTPRRGRDFGGALYGKQGTVEVADQLRGVAWLKQQPWVD PARIGVQGWSNGGYMTLMLLAKASDSYACGVAGAPVTDWGLYDSHYTERY MDLPARNDAGYREARVLTHIEGLRSPLLLIHGMADDNVLFTNSTSLMSAL QKRGQPFELMTYPGAKHGLSGADALHRYRVAEAFLGRCLKP
BACKGROUND: Stenotrophomonas maltophilia is a nosocomial opportunistic pathogen of the Xanthomonadaceae. The organism has been isolated from both clinical and soil environments in addition to the sputum of cystic fibrosis patients and the immunocompromised. Whilst relatively distant phylogenetically, the closest sequenced relatives of S. maltophilia are the plant pathogenic xanthomonads. RESULTS: The genome of the bacteremia-associated isolate S. maltophilia K279a is 4,851,126 bp and of high G+C content. The sequence reveals an organism with a remarkable capacity for drug and heavy metal resistance. In addition to a number of genes conferring resistance to antimicrobial drugs of different classes via alternative mechanisms, nine resistance-nodulation-division (RND)-type putative antimicrobial efflux systems are present. Functional genomic analysis confirms a role in drug resistance for several of the novel RND efflux pumps. S. maltophilia possesses potentially mobile regions of DNA and encodes a number of pili and fimbriae likely to be involved in adhesion and biofilm formation that may also contribute to increased antimicrobial drug resistance. CONCLUSION: The panoply of antimicrobial drug resistance genes and mobile genetic elements found suggests that the organism can act as a reservoir of antimicrobial drug resistance determinants in a clinical environment, which is an issue of considerable concern.
The crystal structure of dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia was determined at 2.8-A resolution by the multiple isomorphous replacement method, using platinum and selenomethionine derivatives. The crystals belong to space group P4(3)2(1)2, with unit cell parameters a = b = 105.9 A and c = 161.9 A. Dipeptidyl aminopeptidase IV is a homodimer, and the subunit structure is composed of two domains, namely, N-terminal beta-propeller and C-terminal catalytic domains. At the active site, a hydrophobic pocket to accommodate a proline residue of the substrate is conserved as well as those of mammalian enzymes. Stenotrophomonas dipeptidyl aminopeptidase IV exhibited activity toward a substrate containing a 4-hydroxyproline residue at the second position from the N terminus. In the Stenotrophomonas enzyme, one of the residues composing the hydrophobic pocket at the active site is changed to Asn611 from the corresponding residue of Tyr631 in the porcine enzyme, which showed very low activity against the substrate containing 4-hydroxyproline. The N611Y mutant enzyme was generated by site-directed mutagenesis. The activity of this mutant enzyme toward a substrate containing 4-hydroxyproline decreased to 30.6% of that of the wild-type enzyme. Accordingly, it was considered that Asn611 would be one of the major factors involved in the recognition of substrates containing 4-hydroxyproline.
Title: Dipeptidyl peptidase IV from Xanthomonas maltophilia: sequencing and expression of the enzyme gene and characterization of the expressed enzyme Kabashima T, Ito K, Yoshimoto T Ref: J Biochem, 120:1111, 1996 : PubMed
The dipeptidyl peptidase IV [EC 3.4.14.5] gene of Xanthomonas maltophilia, expressed in Escherichia coli, was cloned by the shotgun method. Nucleotide sequence analysis revealed an open reading frame of 2,223 bp, coding for a protein of 741 amino acids with a predicted molecular weight of 82,080. The expressed enzyme was extracted with SDS, and the solubilized enzyme was purified about 1,030-fold on columns of Toyopearl HW65C, DEAE-Toyopearl twice, and hydroxyapatite, with an activity recovery of 50%. The enzyme hydrolyzed a proline-containing peptide at the penultimate position, and was inhibited by diisopropyl phosphofluoridate. The enzyme was most active at pH 8.5, and was stable between at pH 7.0 and 9.0. The molecular weight of the purified enzyme was estimated to be 83,000 and 165,000 by SDS-PAGE and gel filtration, respectively.
Xanthomonas maltophilia (Pseudomonas maltophilia) dipeptidyl peptidase IV
