STRINGSTRING
dnaA dnaA Sdel_0004 Sdel_0004 gyrB gyrB ung ung Sdel_0010 Sdel_0010 Sdel_0011 Sdel_0011 Sdel_0046 Sdel_0046 gyrA gyrA dnaX dnaX Sdel_0541 Sdel_0541 Sdel_0554 Sdel_0554 polA polA uvrC uvrC Sdel_0632 Sdel_0632 Sdel_0862 Sdel_0862 Sdel_0864 Sdel_0864 Sdel_0925 Sdel_0925 Sdel_0947 Sdel_0947 Sdel_0948 Sdel_0948 Sdel_1231 Sdel_1231 ligA ligA Sdel_1375 Sdel_1375 Sdel_1410 Sdel_1410 Sdel_1522 Sdel_1522 Sdel_1535 Sdel_1535 rpoD rpoD Sdel_1595 Sdel_1595 priA priA uvrB uvrB Sdel_1605 Sdel_1605 Sdel_1633 Sdel_1633 Sdel_1796 Sdel_1796 dnaG dnaG topA topA recA recA Sdel_2254 Sdel_2254
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
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textmining
co-expression
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dnaAChromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family. (441 aa)
Sdel_0004DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] (355 aa)
gyrBDNA gyrase, B subunit; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. (770 aa)
unguracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. (224 aa)
Sdel_0010A/G-specific adenine glycosylase; Adenine glycosylase active on G-A mispairs. (317 aa)
Sdel_0011Hypothetical protein. (38 aa)
Sdel_0046TIGRFAM: single-stranded-DNA-specific exonuclease RecJ; PFAM: phosphoesterase RecJ domain protein; phosphoesterase DHHA1; KEGG: cco:CCC13826_0910 single-stranded-DNA- specific exonuclease RecJ. (527 aa)
gyrADNA gyrase, A subunit; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. (846 aa)
dnaXDNA polymerase III, subunits gamma and tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. (546 aa)
Sdel_0541KEGG: sun:SUN_0644 exodeoxyribonuclease III; TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. (254 aa)
Sdel_0554Excinuclease ABC, A subunit; 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. (938 aa)
polADNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. (885 aa)
uvrCExcinuclease ABC, C subunit; 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. (599 aa)
Sdel_0632KEGG: wsu:WS1983 DNA polymerase III subunit alpha; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein. (1182 aa)
Sdel_0862Single-strand binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. (166 aa)
Sdel_0864PFAM: DNA polymerase III delta; KEGG: sun:SUN_0430 DNA polymerase III subunit delta. (328 aa)
Sdel_0925PFAM: Exonuclease RNase T and DNA polymerase III; SMART: Exonuclease; KEGG: sun:SUN_1076 exonuclease. (246 aa)
Sdel_0947PFAM: metallophosphoesterase; KEGG: sun:SUN_0725 DNA double-strand break repair protein. (372 aa)
Sdel_0948PFAM: SMC domain protein; KEGG: sun:SUN_0726 DNA double-strand break repair protein. (789 aa)
Sdel_1231PFAM: Abortive phage infection; KEGG: nmu:Nmul_A2605 hypothetical protein. (567 aa)
ligADNA ligase, NAD-dependent; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. (648 aa)
Sdel_1375KEGG: abu:Abu_1201 putative DNA polymerase III delta prime subunit HolB. (208 aa)
Sdel_1410PFAM: UvrD/REP helicase; KEGG: ccv:CCV52592_1083 acyl carrier protein. (676 aa)
Sdel_1522PFAM: Ion transport 2 domain protein; KEGG: saz:Sama_2879 uncharacterized low-complexity protein. (302 aa)
Sdel_1535KEGG: sun:SUN_2266 ATP-dependent DNA helicase RecQ; TIGRFAM: ATP-dependent DNA helicase RecQ; ATP- dependent DNA helicase, RecQ family; PFAM: HRDC domain protein; DEAD/DEAH box helicase domain protein; RQC domain; helicase domain protein; SMART: DEAD-like helicase; helicase domain protein; HRDC domain protein. (596 aa)
rpoDRNA polymerase sigma factor RpoD; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. (617 aa)
Sdel_1595Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. Belongs to the helicase family. DnaB subfamily. (476 aa)
priAPrimosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. (611 aa)
uvrBExcinuclease ABC, B subunit; 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 [...] (658 aa)
Sdel_1605KEGG: ccv:CCV52592_0726 DNA polymerase III subunit epsilon; TIGRFAM: DNA polymerase III, epsilon subunit; PFAM: Exonuclease RNase T and DNA polymerase III; SMART: Exonuclease. (260 aa)
Sdel_1633PFAM: UvrD/REP helicase; KEGG: nis:NIS_1473 ATP-dependent DNA helicase UvrD. (681 aa)
Sdel_1796PFAM: ATP dependent DNA ligase; KEGG: msu:MS0939 DNA ligase. (271 aa)
dnaGDNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. (552 aa)
topADNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] (694 aa)
recArecA protein; 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. (347 aa)
Sdel_2254methylated-DNA/protein- cysteinemethyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. (151 aa)
Your Current Organism:
Sulfurospirillum deleyianum
NCBI taxonomy Id: 525898
Other names: S. deleyianum DSM 6946, Sulfurospirillum deleyianum DSM 6946, Sulfurospirillum deleyianum str. DSM 6946, Sulfurospirillum deleyianum strain DSM 6946
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