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Description:
UvrABC system protein B (Protein uvrB) (Excinuclease ABC subunit B).
Molecular weight: 77565
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) base-excision repair( GO:0006284 ) nucleotide-excision repair (and GO:0045001, a synonym)( GO:0006289 )
Important dates:
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
07-MAR-2006, entry version 41.
Phylogenetic order:
Bacteria Spirochaetes Spirochaetales Spirochaetaceae Borrelia Borrelia burgdorferi group.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein UVRB_BORBU:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE001182 | AAC67185.1 | - |
| PIR | C70204 | C70204. | |
| HSSP | P56981 | 1D9X | |
| GenomeReviews | AE000783_GR | BB0836.1 | |
| TIGR | BB0836 | -. | |
| BioCyc | BBUR139:BB0836-MONOMER | -.1 | |
| HAMAP | MF_00204 | - | 1. |
| InterPro | IPR001410 | DEAD. | |
| InterPro | IPR011545 | DEAD/DEAH_N. | |
| InterPro | IPR001650 | Helicase_C. | |
| InterPro | IPR006935 | ResIII. | |
| InterPro | IPR001943 | UvrB/C. | |
| InterPro | IPR004807 | UvrB_ABC. | |
| Pfam | PF00271 | Helicase_C | 1. |
| Pfam | PF04851 | ResIII | 1. |
| Pfam | PF02151 | UVR | 1. |
| SMART | SM00487 | DEXDc | 1. |
| SMART | SM00490 | HELICc | 1. |
| TIGRFAMs | TIGR00631 | uvrb | 1. |
| PROSITE | PS50151 | UVR | 1. |
Keywords:
ATP-binding; Complete proteome; DNA damage; DNA excision; DNA repair; Excision nuclease; Nucleotide-binding; SOS response.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / B31;
RX MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT burgdorferi.";
RL Nature 390:580-586(1997).
Feature:
CHAIN 1 673 UvrABC system protein B.
/FTId=PRO_0000138382.
DOMAIN 627 662 UVR.
NP_BIND 43 50 ATP (Potential).
MOTIF 96 119 Beta-hairpin.
Comments:
-!- 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).
-!- SUBUNIT: Forms a heterotetramer with uvrA during the search for
lesions. Interacts with uvrC in an incision complex (By
similarity).
-!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
-!- DOMAIN: The beta-hairpin motif is involved in DNA binding (By
similarity).
-!- SIMILARITY: Belongs to the uvrB family.
-!- SIMILARITY: Contains 1 UVR domain.
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Sequence length: 673
MVVKLMIDFF LKSEYLPAGD QPKAIKEIEN SILLGNKYQT LKGVTGSGKT FTIANIIKDL
NRPALVVSHN KTLAAQLYRE FKDFFPNNAV EYFVSYYDYY QPESYVPSKD LFIEKEATIN
TEIEIKRIRT VTSLAKRRDV IVVATVSSIY ALGSPDFFKK SAREFFVGQK ISIKEISDIF
VELYYERTLM NLERDKFSIK GDIVEIWPSS EHGEFAYRIC LDFDEIVEIY RVSSFSKKNL
GATNSFTLFA KSYFVIPYEN VLEAIPKISH DLSLQCQYFK DNGKLVEAER LKQRVEYDLE
MLRETGFCSG IENYSKYLSG STMERPYCLF DFFPKDXLLF VDESHVTLPQ FRGMYNGDHS
RKLNLVNFGF RLPAALENRP LKYDEFEALI NQVVFVSATP GVEENEKSSV VVDQIIRPTG
LVDPEIITRH SDGQMEDLYS EIQKRVALKE RVLITTLTKK MSEDLTEYLV NLGVRAKYLH
SELDTLERVE VISLLRKSEI DVIVGINLLR EGLDIPEVSL VAILDADKVG FLRSTTSLIQ
TIGRAARNSN GLVIMYYDKI SLAMREAIEE TNRRRQIQID YNKKNNITPK TIVKKIQNIL
EKELNNKNKN VGYDFEKIIS GERLSKKKLI DKLKFDLEEA VNDERFEDAI VLRDKIKELS
SKISIARNKK REV