| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | UvrABC system protein B |
Protein Synonyms/Alias | Protein UvrB |
Gene Name | uvrB |
Gene Synonyms/Alias | SPD_1096 |
Created Date | 3-June-2014 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
NCBI Taxa ID | 373153 |
Phosphorylation | Position | Peptide | Code | Type | References | | 542 | NERGLIQTIGRAARN | T | HTP | [1] | |
Reference | [1]Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae. Sun X,Ge F,Xiao CL,Yin XF,Ge R,Zhang LH,He QY J. Proteome Res. 2010, Jan;9(1):275-82. [ PMID:19894762] |
Functional Description From UniProt | FUNCTION: 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 and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage (By similarity) |
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| ATP-binding; Completeproteome; Cytoplasm; DNAdamage; DNAexcision; DNArepair; Excisionnuclease; Helicase; Hydrolase; Nucleotide-binding; SOSresponse |
Protein Sequence | MINHITDNQF KLVSKYQPSG DQPQAIEQLV DNIEGGEKAQ ILMGATGTGK TYTMSQVISK 60
VNKPTLVIAH NKTLAGQLYG EFKEFFPENA VEYFVSYYDY YQPEAYVPSS DTYIEKDSSV 120
NDEIDKLRHS ATSALLERND VIVVASVSCI YGLGSPKEYA DSVVSLRPGL EISRDKLLND 180
LVDIQFERND IDFQRGRFRV RGDVVEIFPA SRDEHAFRVE FFGDEIDRIR EVEALTGQVL 240
GEVDHLAIFP ATHFVTNDDH MEVAIAKIQA ELEEQLAVFE KEGKLLEAQR LKQRTEYDIE 300
MLREMGYTNG VENYSRHMDG RSEGEPPYTL LDFFPDDFLI MIDESHMTMG QIKGMYNGDR 360
SRKEMLVNYG FRLPSALDNR PLRREEFESH VHQIVYVSAT PGDYENEQTE TVIEQIIRPT 420
GLLDPEVEVR PTMGQIDDLL GEINARVEKN ERTFITTLTK KMAEDLTDYF KEMGIKVKYM 480
HSDIKTLERT EIIRDLRLGV FDVLVGINLL REGIDVPEVS LVAILDADKE GFLRNERGLI 540
QTIGRAARNS EGHVIMYADT VTQSMQRAID ETARRRKIQM AYNEEHGIVP QTIKKEIRDL 600
IAVTKAVAKE EDKEVDINSL NKQERKELVK KLEKQMQEAV EVLDFELAAQ IRDMMLEVKA 660
LD 662 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0003677 F:DNA binding IEA:UniProtKB-HAMAP GO:0009381 F:excinuclease ABC activity IEA:UniProtKB-HAMAP GO:0004386 F:helicase activity IEA:UniProtKB-HAMAP GO:0006289 P:nucleotide-excision repair IEA:UniProtKB-HAMAP GO:0009432 P:SOS response IEA:UniProtKB-HAMAP |
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