Recombinase A; 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.

DNA-directed DNA polymerase; 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 repl [...]

Excinuclease 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 [...]

Putative DNA-directed polymerase III; Excinuclease cho (EC 3.1.25.-) (Endonuclease cho) (UvrC homolog protein). Incises the DNA at the 3 side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than uvrC. Not able to incise the 5 site of a lesion. When a lesion remains because uvrC is not able to induce the 3 incision cho incises the DNA. Then uvrC makes the 5 incision. The combined action of cho and uvrC broadens the substrate range of nucleotide excision repair (By similarity); Specificity unclear.

DNA mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.

DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.

Putative phasin protein PhaP.A family of small proteins found associated with inclusions in bacterial cells. Most associate with polyhydroxyalkanoate (PHA) inclusions, the most common of which consist of polyhydroxybutyrate (PHB). These are designated granule-associate proteins or phasins. However, the member from Magnetospirillum sp. AMB-1 is called a magnetic particle membrane-specific GTPase. TrEMBL: Q93QF2 InterPro:IPR010127,TIGR01841 NO TMH Present No Signal Peptide Present; Family membership.

DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...]

DNA helicase, ATP-dependent dsDNA/ssDNA exonuclease V subunit, ssDNA endonuclease; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the [...]