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Description:
UvrABC system protein B (Protein uvrB) (Excinuclease ABC subunit B).
Molecular weight: 76095
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:
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 1.
07-MAR-2006, entry version 14.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
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_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X03678 | CAA27314.1 | - |
| EMBL | X03722 | CAA27357.1 | - |
| EMBL | U00096 | AAC73866.1 | - |
| EMBL | D90716 | BAA35437.1 | - |
| PIR | A93613 | BVECUB. | |
| PDB | 1E52 | NMR | A/B=618-672. |
| PDB | 1QOJ | X-ray | A/B=618-672. |
| ECO2DBASE | C080.0 | 6TH EDITION. | |
| GenomeReviews | U00096_GR | b0779.1 | |
| EchoBASE | EB1055 | -.1 | |
| EcoGene | EG11062 | uvrB. | |
| GO | GO:0005515 | F:protein binding | IPI. |
| HAMAP | MF_00204 | - | 1. |
| InterPro | IPR001410 | DEAD. | |
| InterPro | IPR011545 | DEAD/DEAH_N. | |
| InterPro | IPR001650 | Helicase_C. | |
| 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:
3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; DNA damage; DNA excision; DNA repair; Excision nuclease; Nucleotide-binding; SOS response.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7, AND
RP PROTEOLYTIC PRODUCT.
RC STRAIN=K12;
RX MEDLINE=86176755; PubMed=3515321;
RA Arikan E., Kulkarni M.S., Thomas D.C., Sancar A.;
RT "Sequences of the E. coli uvrB gene and protein.";
RL Nucleic Acids Res. 14:2637-2650(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=86176773; PubMed=3008099;
RA Backendorf C., Spaik H., Barbeiro A.P., van de Putte P.;
RT "Structure of the uvrB gene of Escherichia coli. Homology with other
RT DNA repair enzymes and characterization of the uvrB5 mutation.";
RL Nucleic Acids Res. 14:2877-2890(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-672.
RC STRAIN=K12 / W3110;
RX MEDLINE=97061202; PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA Yano M., Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP FUNCTION, AND DIMERIC STATE OF UVRB.
RX MEDLINE=22140055; PubMed=12145219; DOI=10.1093/emboj/cdf396;
RA Verhoeven E.E., Wyman C., Moolenaar G.F., Goosen N.;
RT "The presence of two UvrB subunits in the UvrAB complex ensures damage
RT detection in both DNA strands.";
RL EMBO J. 21:4196-4205(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 618-672.
RX MEDLINE=20123894; PubMed=10631326; DOI=10.1016/S0014-5793(99)01690-7;
RA Sohi M., Alexandrovich A., Moolenaar G., Visse R., Goosen N.,
RA Vernede X., Fontecilla-Camps J.-C., Champness J., Sanderson M.R.;
RT "Crystal structure of Escherichia coli UvrB C-terminal domain, and a
RT model for UvrB-uvrC interaction.";
RL FEBS Lett. 465:161-164(2000).
RN [7]
RP STRUCTURE BY NMR OF 618-672.
RX MEDLINE=99297571; PubMed=10371161; DOI=10.1016/S0014-5793(99)00542-6;
RA Alexandrovich A., Sanderson M.R., Moolenaar G.F., Goosen N.,
RA Lane A.N.;
RT "NMR assignments and secondary structure of the UvrC binding domain of
RT UvrB.";
RL FEBS Lett. 451:181-185(1999).
RN [8]
RP MUTAGENESIS OF TYR-94; TYR-95; TYR-100 AND PHE-107.
RX MEDLINE=21547950; PubMed=11689453; DOI=10.1093/emboj/20.21.6140;
RA Moolenaar G.F., Hoeglund L., Goosen N.;
RT "Clue to damage recognition by UvrB: residues in the beta-hairpin
RT structure prevent binding to non-damaged DNA.";
RL EMBO J. 20:6140-6149(2001).
Feature:
INIT_MET 0 0
CHAIN 1 672 UvrABC system protein B.
/FTId=PRO_0000138390.
DOMAIN 632 667 UVR.
NP_BIND 38 45 ATP (Potential).
MOTIF 91 114 Beta-hairpin.
SITE 629 630 Cleavage (Potential).
MUTAGEN 94 95 YY->AA: Defective in DNA-unwinding
activity.
MUTAGEN 100 100 Y->A: Defective in DNA-unwinding
activity; when associated with A-108.
MUTAGEN 107 107 F->A: Defective in DNA-unwinding
activity; when associated with A-101.
CONFLICT 476 476 H -> R (in Ref. 1).
HELIX 628 647
TURN 648 649
TURN 651 652
HELIX 653 670
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.
-!- SUBUNIT: Forms a heterotetramer with uvrA during the search for
lesions. Interacts with uvrC in an incision complex.
-!- INTERACTION:
P06959:aceF; NbExp=1; IntAct=EBI-552176, EBI-542707;
P23524:garK; NbExp=1; IntAct=EBI-552176, EBI-562100;
P08936:hns; NbExp=1; IntAct=EBI-552176, EBI-544934;
P10484:hsdM; NbExp=1; IntAct=EBI-552176, EBI-552119;
P02342:hupA; NbExp=1; IntAct=EBI-552176, EBI-547648;
P02341:hupB; NbExp=1; IntAct=EBI-552176, EBI-370411;
P00391:lpdA; NbExp=1; IntAct=EBI-552176, EBI-542856;
P68739:nfi; NbExp=1; IntAct=EBI-552176, EBI-551698;
P0A7M2:rpmB; NbExp=1; IntAct=EBI-552176, EBI-543024;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
-!- MISCELLANEOUS: According to Ref.1, a cleaved form of the protein
was observed that resulted from the removal of about 40 amino
acids from the C-terminus of the protein. The exact cleavage site
being unknown, it was proposed to be between Lys-629 and Ala-630.
There was no indication that cleavage occured in vivo and
therefore it is not known if it has any physiological
significance.
-!- SIMILARITY: Belongs to the uvrB family.
-!- SIMILARITY: Contains 1 UVR domain.
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Sequence length: 672
SKPFKLNSAF KPSGDQPEAI RRLEEGLEDG LAHQTLLGVT GSGKTFTIAN VIADLQRPTM
VLAPNKTLAA QLYGEMKEFF PENAVEYFVS YYDYYQPEAY VPSSDTFIEK DASVNEHIEQ
MRLSATKAML ERRDVVVVAS VSAIYGLGDP DLYLKMMLHL TVGMIIDQRA ILRRLAELQY
ARNDQAFQRG TFRVRGEVID IFPAESDDIA LRVELFDEEV ERLSLFDPLT GQIVSTIPRF
TIYPKTHYVT PRERIVQAME EIKEELAARR KVLLENNKLL EEQRLTQRTQ FDLEMMNELG
YCSGIENYSR FLSGRGPGEP PPTLFDYLPA DGLLVVDESH VTIPQIGGMY RGDRARKETL
VEYGFRLPSA LDNRPLKFEE FEALAPQTIY VSATPGNYEL EKSGGDVVDQ VVRPTGLLDP
IIEVRPVATQ VDDLLSEIRQ RAAINERVLV TTLTKRMAED LTEYLEEHGE RVRYLHSDID
TVERMEIIRD LRLGEFDVLV GINLLREGLD MPEVSLVAIL DADKEGFLRS ERSLIQTIGR
AARNVNGKAI LYGDKITPSM AKAIGETERR REKQQKYNEE HGITPQGLNK KVVDILALGQ
NIAKTKAKGR GKSRPIVEPD NVPMDMSPKA LQQKIHELEG LMMQHAQNLE FEEAAQIRDQ
LHQLRELFIA AS