Thermus thermophilus proline iminopeptidase (EC 3.4.11.5) (no catalytic serine)
Comment
Other strains: Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)(strain HB8 / ATCC 27634 / DSM 579). The residue corresponding to the catalytic Ser105 in F1 is replaced by a Gly at TTHA1809
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Deinococcus-Thermus: NE > Deinococci: NE > Thermales: NE > Thermaceae: NE > Thermus: NE > Thermus thermophilus: 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.) Thermus thermophilus HB8: N, E.
Thermus thermophilus HB27: N, E.
Molecular evidence
Database
No mutation 1 structure: 2YYS: Crystal structure of the proline iminopeptidase-related protein TTHA1809 from Thermus thermophilus HB8 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 MREEIGYVPVGEAELYVEDVGPVEGPALLVLHGGPGGNAYVLREGLQDYL EGFRVVYFDQRGSGRSLELPQDPRLFTVDALVEDTLLLAEALGVERFGLL AHGFGAVVALEVLRRFPQAEGAILLAPWVNFPWLAARLAEAAGLAPLPDP EENLKEALKREEPKALFDRLMFPTPRGRMAYEWLAEGAGILGSDAPGLAF LRNGLWRLDYTPYLTPERRPLYVLVGERDGTSYPYAEEVASRLRAPIRVL PEAGHYPWIDAPEAFEEAFKEALAALVPALRGPLVD
Thermus thermophilus HB8, an extremely thermophilic bacterium. The open reading frame of TTHA1809 from Thermus thermophilus HB8 was annotated as a proline iminopeptidase-related protein. Proline iminopeptidase (PIP) is a serine peptidase that catalyzes the removal of N-terminal proline from peptides with high specificity. In this study, we report the crystal structure of the proline iminopeptidase-related protein TTHA1809 from Thermus thermophilus HB8, and compare the active site of the tricorn-interacting aminopeptidase F1, which is the best homolog found using the Dali program, with the corresponding region of TTHA1809. Comparison with the tricorn-interacting aminopeptidase F1: The tricorn-interacting aminopeptidase F120 from Thermoplasma acidophilum has a Ser-His-Asp catalytic triad in the active site. The superimposition between TTHA1809 and F1 revealed that the residue corresponding to the catalytic Ser105 in F1 is replaced by a Gly at TTHA1809. Asp229 and His255 of TTHA1809 were located at the same position as Asp244 and His271 of the catalytic triad of F1. His255 of TTHA1809 was located in a loop between the beta8-strand and the alpha10-helix. The ND-1 atom of His255 was hydrogen-bonded to Asp229 in a loop located between the beta7-strand and the alpha9-helix, whereas the NE-2 atom of His255 formed a hydrogen bond with a water molecule because of the lack of catalytic Ser residue. Thus, TTHA1809 and F1 would have different functions. A BLAST search using TTHA1809 revealed the possibility of the existence of enzymes lacking a catalytic Ser residue in several microorganisms (Thermus thermophilus HB27, Deinococcus geothermalis DSM 11300, Legionella pneumophila subsp. pneumophila str. Philadelphia 1, Dechloromonas aromatica RCB, and Hahella chejuensis KCTC 2396), but their functions have not yet been revealed.
Thermus thermophilus HB27 is an extremely thermophilic, halotolerant bacterium, which was originally isolated from a natural thermal environment in Japan. This organism has considerable biotechnological potential; many thermostable proteins isolated from members of the genus Thermus are indispensable in research and in industrial applications. We present here the complete genome sequence of T. thermophilus HB27, the first for the genus Thermus. The genome consists of a 1,894,877 base pair chromosome and a 232,605 base pair megaplasmid, designated pTT27. The 2,218 identified putative genes were compared to those of the closest relative sequenced so far, the mesophilic bacterium Deinococcus radiodurans. Both organisms share a similar set of proteins, although their genomes lack extensive synteny. Many new genes of potential interest for biotechnological applications were found in T. thermophilus HB27. Candidates include various proteases and key enzymes of other fundamental biological processes such as DNA replication, DNA repair and RNA maturation.
Thermus thermophilus proline iminopeptidase (EC 3.4.11.5) (no catalytic serine)
