STRINGSTRING
Sps_05110 Sps_05110 recF recF Sps_00264 Sps_00264 lexA lexA Sps_00586 Sps_00586 uvrC uvrC Sps_00798 Sps_00798 Sps_01021 Sps_01021 Sps_01022 Sps_01022 uvrB uvrB ruvB ruvB ruvA ruvA Sps_01173 Sps_01173 uvrA uvrA Sps_03292 Sps_03292 Sps_03454 Sps_03454 recA recA dinB dinB
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_05110PFAM: Protein of unknown function (DUF461). (153 aa)
recFDNA replication and repair protein RecF; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP; Belongs to the RecF family. (365 aa)
Sps_00264Cell division inhibitor SulA; Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division. (170 aa)
lexASOS-response transcriptional repressor, LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. (205 aa)
Sps_00586PFAM: YebG protein. (101 aa)
uvrCExcinuclease ABC subunit C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. (609 aa)
Sps_00798ATP-dependent DNA helicase, RecQ-like; PFAM: Helicase conserved C-terminal domain; DEAD/DEAH box helicase; 'TIGRFAM: ATP-dependent DNA helicase, RecQ family'. (654 aa)
Sps_01021PFAM: Peptidase S24-like; Belongs to the peptidase S24 family. (144 aa)
Sps_01022nucleotidyltransferase/DNA polymerase involved in DNA repair; PFAM: Domain of unknown function (DUF4113); impB/mucB/samB family C-terminal domain; impB/mucB/samB family. (417 aa)
uvrBExcinuclease ABC subunit B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] (671 aa)
ruvBHolliday junction DNA helicase subunit RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. (339 aa)
ruvAHolliday junction DNA helicase subunit RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. (205 aa)
Sps_01173alpha-L-glutamate ligase-related protein; PFAM: Sugar-transfer associated ATP-grasp; TIGRFAM: alpha-L-glutamate ligase-related protein. (320 aa)
uvrAExcinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. (944 aa)
Sps_03292ATP-dependent DNA helicase RecQ; PFAM: Helicase conserved C-terminal domain; RQC domain; HRDC domain; DEAD/DEAH box helicase; 'TIGRFAM: ATP-dependent DNA helicase RecQ; ATP-dependent DNA helicase, RecQ family'. (608 aa)
Sps_03454Hypothetical protein. (293 aa)
recAProtein RecA; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. (352 aa)
dinBnucleotidyltransferase/DNA polymerase involved in DNA repair; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. (353 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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