Literature DB >> 25428979

Draft Genome Sequence of Chryseobacterium sp. Strain P1-3, a Keratinolytic Bacterium Isolated from Poultry Waste.

Gun-Seok Park1, Sung-Jun Hong1, Chang-Hyun Lee1, Abdur Rahim Khan1, Ihsan Ullah1, Byung Kwon Jung1, JungBae Choi1, Yunyoung Kwak1, Chang-Gi Back1, Hee-Young Jung1, Jae-Ho Shin2.   

Abstract

Chryseobacterium sp. strain P1-3, harboring keratin degrading activity, has recently been isolated from poultry waste. Here, we report the 4.6-Mbp draft genome sequence of the keratinolytic bacterium with a G+C content of 37.0% and 4,087 protein-coding genes.
Copyright © 2014 Park et al.

Entities:  

Year:  2014        PMID: 25428979      PMCID: PMC4246171          DOI: 10.1128/genomeA.01237-14

Source DB:  PubMed          Journal:  Genome Announc


GENOME ANNOUNCEMENT

Keratin, the major component of animal hair, nail, feathers, and wool, is the most abundant fibrous protein in the epithelial cells of vertebrates (1). The insoluble protein is tightly packed in an α-helix structure (α-keratin) or β-sheet structure (β-keratin) into a supercoiled polypeptide chain with cysteine bridges (2). Keratin shows resistance to proteolysis due not only to the disulfide bonds, but also to the structurally limited interior space with hydrophobic interactions between nonpolar residues (3). The proteolytic resistance of keratin has been considered to be a critical factor disturbing the process of keratin waste treatment (4). To date, some keratinolytic microorganisms producing various proteases have been reported, such as Bacillus (5), fungi (6), thermophilic bacteria (7), and even Chryseobacterium (8). The keratinolytic proteases from these organisms may have important uses for the biodegradation of keratin-containing waste from industry (9). The genus Chryseobacterium, belonging to a member of family Flavobacteriaceae, is a non-spore-forming, nonmotile, rod-shaped Gram-negative bacterium. Chryseobacterium species have been known to possess strong proteolytic activity with typical morphological characteristics, such as translucent circular and yellow pigmented colonies (10). A strong keratin degrader, strain Chryseobacterium sp. P1-3 was isolated from a poultry waste dumping ground in Iksan, Jeonbuk, Republic of Korea (S. J. Hong, unpublished data). The genomic DNA of the strain P1-3 was sequenced to enlarge the enzymatic hydrolysis efficacy for keratin waste treatment. The genome was sequenced using an Ion Torrent personal genome machine (PGM) sequencer with a 316 v2 chip (11). The sequence reads were assembled using Mimicking Intelligent Read Assembly (MIRA) 4.0 (12). The draft genome is composed of 45 contigs (>728 bp). The genome size is 4,628,764 bp at 78.0-fold coverage with a G+C content of 37.0%. The assembled contigs were annotated using the Prokaryotic Genome Annotation Pipeline (PGAP) version 2.6 software on NCBI (http://www.ncbi.nlm.nih.gov/genome/annotation_prok/) and the Rapid Annotation using Subsystem Technology (RAST) server (13). The genome contains a total of 4,087 genes, consisting of 3,119 protein-coding sequences (CDSs), 882 pseudo genes, 20 rRNA (5S, 16S, 23S) genes, 65 tRNA genes, and 1 ncRNA gene. Predicted genes were functionally assigned via 311 RAST subsystems. In regard to the keratinolytic activity, a total of 32 open reading frames are identified as proteases, including metalloproteases and serine proteases. The genome sequence of Chryseobacterium sp. strain P1-3 may contribute to a better understanding of keratin degradation and also provide potential applications for the treatment of keratin wastes.

Nucleotide sequence accession number.

The draft genome sequence of strain Chryseobacterium sp. P1-3 has been deposited at DDBJ/EMBL/GenBank under the accession no. JPEQ00000000.
  10 in total

1.  Keratinase of Doratomyces microsporus.

Authors:  H Gradisar; S Kern; J Friedrich
Journal:  Appl Microbiol Biotechnol       Date:  2000-02       Impact factor: 4.813

2.  Novel keratinase from Bacillus subtilis S14 exhibiting remarkable dehairing capabilities.

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Journal:  Appl Environ Microbiol       Date:  2005-01       Impact factor: 4.792

3.  Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. kr6.

Authors:  Alessandro Riffel; Adriano Brandelli; Cláudia de M Bellato; Gustavo H M F Souza; Marcos N Eberlin; Flavio C A Tavares
Journal:  J Biotechnol       Date:  2006-11-18       Impact factor: 3.307

4.  Proteopedia entry: coiled-coil structure of keratins.

Authors:  Israel Hanukoglu; Liora Ezra
Journal:  Biochem Mol Biol Educ       Date:  2013-11-22       Impact factor: 1.160

5.  An integrated semiconductor device enabling non-optical genome sequencing.

Authors:  Jonathan M Rothberg; Wolfgang Hinz; Todd M Rearick; Jonathan Schultz; William Mileski; Mel Davey; John H Leamon; Kim Johnson; Mark J Milgrew; Matthew Edwards; Jeremy Hoon; Jan F Simons; David Marran; Jason W Myers; John F Davidson; Annika Branting; John R Nobile; Bernard P Puc; David Light; Travis A Clark; Martin Huber; Jeffrey T Branciforte; Isaac B Stoner; Simon E Cawley; Michael Lyons; Yutao Fu; Nils Homer; Marina Sedova; Xin Miao; Brian Reed; Jeffrey Sabina; Erika Feierstein; Michelle Schorn; Mohammad Alanjary; Eileen Dimalanta; Devin Dressman; Rachel Kasinskas; Tanya Sokolsky; Jacqueline A Fidanza; Eugeni Namsaraev; Kevin J McKernan; Alan Williams; G Thomas Roth; James Bustillo
Journal:  Nature       Date:  2011-07-20       Impact factor: 49.962

6.  Similarities and specificities of fungal keratinolytic proteases: comparison of keratinases of Paecilomyces marquandii and Doratomyces microsporus to some known proteases.

Authors:  Helena Gradisar; Jozica Friedrich; Igor Krizaj; Roman Jerala
Journal:  Appl Environ Microbiol       Date:  2005-07       Impact factor: 4.792

Review 7.  Biodegradation of keratin waste: Theory and practical aspects.

Authors:  Teresa Korniłłowicz-Kowalska; Justyna Bohacz
Journal:  Waste Manag       Date:  2011-05-06       Impact factor: 7.145

8.  Isolation of Thermoanaerobacter keratinophilus sp. nov., a novel thermophilic, anaerobic bacterium with keratinolytic activity.

Authors:  S Riessen; G Antranikian
Journal:  Extremophiles       Date:  2001-12       Impact factor: 2.395

Review 9.  Hard alpha-keratin intermediate filament chains: substructure of the N- and C-terminal domains and the predicted structure and function of the C-terminal domains of type I and type II chains.

Authors:  D A Parry; A C North
Journal:  J Struct Biol       Date:  1998       Impact factor: 2.867

10.  The RAST Server: rapid annotations using subsystems technology.

Authors:  Ramy K Aziz; Daniela Bartels; Aaron A Best; Matthew DeJongh; Terrence Disz; Robert A Edwards; Kevin Formsma; Svetlana Gerdes; Elizabeth M Glass; Michael Kubal; Folker Meyer; Gary J Olsen; Robert Olson; Andrei L Osterman; Ross A Overbeek; Leslie K McNeil; Daniel Paarmann; Tobias Paczian; Bruce Parrello; Gordon D Pusch; Claudia Reich; Rick Stevens; Olga Vassieva; Veronika Vonstein; Andreas Wilke; Olga Zagnitko
Journal:  BMC Genomics       Date:  2008-02-08       Impact factor: 3.969

  10 in total
  5 in total

Review 1.  Microbial decomposition of keratin in nature-a new hypothesis of industrial relevance.

Authors:  Lene Lange; Yuhong Huang; Peter Kamp Busk
Journal:  Appl Microbiol Biotechnol       Date:  2016-01-12       Impact factor: 4.813

2.  Draft Genome Sequence of Chryseobacterium sp. JV274 Isolated from Maize Rhizosphere.

Authors:  Jordan Vacheron; Audrey Dubost; David Chapulliot; Claire Prigent-Combaret; Daniel Muller
Journal:  Genome Announc       Date:  2017-04-13

3.  Comparative Genomics Analysis of Keratin-Degrading Chryseobacterium Species Reveals Their Keratinolytic Potential for Secondary Metabolite Production.

Authors:  Dingrong Kang; Saeed Shoaie; Samuel Jacquiod; Søren J Sørensen; Rodrigo Ledesma-Amaro
Journal:  Microorganisms       Date:  2021-05-12

4.  An Integrative Bioinformatic Analysis for Keratinase Detection in Marine-Derived Streptomyces.

Authors:  Ricardo Valencia; Valentina González; Agustina Undabarrena; Leonardo Zamora-Leiva; Juan A Ugalde; Beatriz Cámara
Journal:  Mar Drugs       Date:  2021-05-21       Impact factor: 5.118

5.  Genome assembly of Chryseobacterium sp. strain IHBB 10212 from glacier top-surface soil in the Indian trans-Himalayas with potential for hydrolytic enzymes.

Authors:  Mohinder Pal; Mohit Kumar Swarnkar; Hena Dhar; Sanjay Chhibber; Arvind Gulati
Journal:  Genom Data       Date:  2017-07-01
  5 in total

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