STRINGSTRING
Sps_00897 Sps_00897 Sps_04294 Sps_04294 Sps_04293 Sps_04293 Sps_02005 Sps_02005 Sps_04385 Sps_04385 Sps_05472 Sps_05472 Sps_00808 Sps_00808 Sps_01891 Sps_01891 Sps_00896 Sps_00896
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Sps_00897Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. (156 aa)
Sps_04294Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. (156 aa)
Sps_04293Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. (155 aa)
Sps_02005Hydroxylase for synthesis of 2-methylthio-cis-ribozeatin in tRNA; PFAM: tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE). (190 aa)
Sps_04385DNA-binding ferritin-like protein (oxidative damage protectant); PFAM: Ferritin-like domain; Belongs to the Dps family. (155 aa)
Sps_05472Ferritin-like protein; Iron-storage protein. (175 aa)
Sps_00808Ribonucleoside-diphosphate reductase class Ia beta subunit; 'PFAM: Ribonucleotide reductase, small chain'. (376 aa)
Sps_01891Hydroxylase for synthesis of 2-methylthio-cis-ribozeatin in tRNA; PFAM: tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE). (262 aa)
Sps_00896Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. (160 aa)
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
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