Cloning and sequence analysis of a putative cell division protein gene ftsK of Streptococcus sobrinus

Ling Yun Su, Bu Ling Wu, Fu Yang Li, Wen Hong Zhang, Ji Hong Fan

Research output: Contribution to journalArticle

Abstract

Objective: To clone and analyze a putative cell division protein gene fisK of Streptococcus sobrinus. Methods A putative cell division protein gene ftsK of Streptococcus sobrinus was cloned by "genome walking system" and PCR amplification. The nucleic acid sequence and amino acid sequence were compared with GenBank, and the amino acid sequence was analyzed by protein analysis software. Results: The gene was consisted of 2100 bp nucleotides which encode 699 amino acids. The secondary structure of the putative S. sobrinus fisK was predicted by GOR4 software. The results showed that the secondary structure of the putative S. sobrinus ftsK was composed mostly of alpha helix and random coil. There were a few extended strands but no beta turns. There was a membrane-spanning region in the N-terminal domain. When the conserved region of amino acid sequence was analyzed, we found that amino acid sequence 335-530 had the conserved region of ftsK/Spo III E. Homology analysis demonstrated that the rest amino acid sequences were homologous to C-terminal 2/3 sequences of E. coli ftsK, except 226 amino acid sequences of N-terminal domain. Amino acid sequences 217-635 were homologous to Spo III E gene of B. subtilis. From 1 to 65 amino acid sequences were homologous to N-terminal domain of Spo III E. Conclusion: The gene cloned in this experiment was a putative cell division protein FtsK of Streptococcus sobrinus.

Original languageEnglish (US)
Pages (from-to)379-382
Number of pages4
JournalChinese Journal of Microbiology and Immunology
Volume25
Issue number5
StatePublished - May 2005
Externally publishedYes

Fingerprint

Streptococcus sobrinus
Cell Division
Sequence Analysis
Organism Cloning
Amino Acid Sequence
Amino Acid Sequence Homology
Proteins
Software
Genes
Nucleic Acid Databases
Nucleic Acids
Walking
Nucleotides
Clone Cells
Genome
Escherichia coli
Amino Acids
Polymerase Chain Reaction
Membranes

Keywords

  • Cell division
  • Cloning
  • ftsK gene
  • Streptococcus sobrinus

ASJC Scopus subject areas

  • Immunology and Microbiology(all)
  • Microbiology (medical)

Cite this

Cloning and sequence analysis of a putative cell division protein gene ftsK of Streptococcus sobrinus. / Su, Ling Yun; Wu, Bu Ling; Li, Fu Yang; Zhang, Wen Hong; Fan, Ji Hong.

In: Chinese Journal of Microbiology and Immunology, Vol. 25, No. 5, 05.2005, p. 379-382.

Research output: Contribution to journalArticle

Su, Ling Yun ; Wu, Bu Ling ; Li, Fu Yang ; Zhang, Wen Hong ; Fan, Ji Hong. / Cloning and sequence analysis of a putative cell division protein gene ftsK of Streptococcus sobrinus. In: Chinese Journal of Microbiology and Immunology. 2005 ; Vol. 25, No. 5. pp. 379-382.
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AU - Zhang, Wen Hong

AU - Fan, Ji Hong

PY - 2005/5

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N2 - Objective: To clone and analyze a putative cell division protein gene fisK of Streptococcus sobrinus. Methods A putative cell division protein gene ftsK of Streptococcus sobrinus was cloned by "genome walking system" and PCR amplification. The nucleic acid sequence and amino acid sequence were compared with GenBank, and the amino acid sequence was analyzed by protein analysis software. Results: The gene was consisted of 2100 bp nucleotides which encode 699 amino acids. The secondary structure of the putative S. sobrinus fisK was predicted by GOR4 software. The results showed that the secondary structure of the putative S. sobrinus ftsK was composed mostly of alpha helix and random coil. There were a few extended strands but no beta turns. There was a membrane-spanning region in the N-terminal domain. When the conserved region of amino acid sequence was analyzed, we found that amino acid sequence 335-530 had the conserved region of ftsK/Spo III E. Homology analysis demonstrated that the rest amino acid sequences were homologous to C-terminal 2/3 sequences of E. coli ftsK, except 226 amino acid sequences of N-terminal domain. Amino acid sequences 217-635 were homologous to Spo III E gene of B. subtilis. From 1 to 65 amino acid sequences were homologous to N-terminal domain of Spo III E. Conclusion: The gene cloned in this experiment was a putative cell division protein FtsK of Streptococcus sobrinus.

AB - Objective: To clone and analyze a putative cell division protein gene fisK of Streptococcus sobrinus. Methods A putative cell division protein gene ftsK of Streptococcus sobrinus was cloned by "genome walking system" and PCR amplification. The nucleic acid sequence and amino acid sequence were compared with GenBank, and the amino acid sequence was analyzed by protein analysis software. Results: The gene was consisted of 2100 bp nucleotides which encode 699 amino acids. The secondary structure of the putative S. sobrinus fisK was predicted by GOR4 software. The results showed that the secondary structure of the putative S. sobrinus ftsK was composed mostly of alpha helix and random coil. There were a few extended strands but no beta turns. There was a membrane-spanning region in the N-terminal domain. When the conserved region of amino acid sequence was analyzed, we found that amino acid sequence 335-530 had the conserved region of ftsK/Spo III E. Homology analysis demonstrated that the rest amino acid sequences were homologous to C-terminal 2/3 sequences of E. coli ftsK, except 226 amino acid sequences of N-terminal domain. Amino acid sequences 217-635 were homologous to Spo III E gene of B. subtilis. From 1 to 65 amino acid sequences were homologous to N-terminal domain of Spo III E. Conclusion: The gene cloned in this experiment was a putative cell division protein FtsK of Streptococcus sobrinus.

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