P0A8F8 (UVRB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UvrABC system protein B
Short name=Protein UvrB

Alternative name(s):
Excinuclease ABC subunit B

Gene names

Name:	uvrB
Ordered Locus Names:	b0779, JW0762

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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 UvrA2B2 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. Ref.7
Subunit structure	Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.
Subcellular location	Cytoplasm HAMAP-Rule MF_00204.
Domain	The beta-hairpin motif is involved in DNA binding. HAMAP-Rule MF_00204
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-630 and Ala-631. There was no indication that cleavage occured in vivo and therefore it is not known if it has any physiological significance. HAMAP-Rule MF_00204
Sequence similarities	Belongs to the UvrB family. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 UVR domain.

Ontologies

Keywords
Biological process	DNA damage DNA excision DNA repair SOS response
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Excision nuclease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SOS response Inferred from electronic annotation. Source: HAMAP nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC nucleotide-excision repair Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP DNA binding Inferred from electronic annotation. Source: HAMAP excinuclease ABC activity Inferred from electronic annotation. Source: HAMAP helicase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 673

672

UvrABC system protein B HAMAP-Rule MF_00204

PRO_0000138390

Regions

Domain

26 – 415

390

Helicase ATP-binding

Domain

431 – 597

167

Helicase C-terminal

Domain

633 – 668

36

UVR

Nucleotide binding

39 – 46

8

ATP Potential

Motif

92 – 115

24

Beta-hairpin HAMAP-Rule MF_00204

Sites

Site

630 – 631

2

Cleavage Potential

Experimental info

Mutagenesis

95 – 96

2

YY → AA: Defective in DNA-unwinding activity.

Mutagenesis

101

1

Y → A: Defective in DNA-unwinding activity; when associated with A-108. Ref.10

Mutagenesis

108

1

F → A: Defective in DNA-unwinding activity; when associated with A-101. Ref.10

Sequence conflict

477

1

H → R in CAA27314. Ref.1

Secondary structure

1

.

.

.

.

.

673

Helix Strand Turn

Details...

Helix

629 – 648

20

Helix

654 – 671

18

Sequences

	Sequence		Length	Mass (Da)
	P0A8F8 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 2F172045344FDAD7	FASTA	673	76,226
	10 20 30 40 50 60 MSKPFKLNSA FKPSGDQPEA IRRLEEGLED GLAHQTLLGV TGSGKTFTIA NVIADLQRPT 70 80 90 100 110 120 MVLAPNKTLA AQLYGEMKEF FPENAVEYFV SYYDYYQPEA YVPSSDTFIE KDASVNEHIE 130 140 150 160 170 180 QMRLSATKAM LERRDVVVVA SVSAIYGLGD PDLYLKMMLH LTVGMIIDQR AILRRLAELQ 190 200 210 220 230 240 YARNDQAFQR GTFRVRGEVI DIFPAESDDI ALRVELFDEE VERLSLFDPL TGQIVSTIPR 250 260 270 280 290 300 FTIYPKTHYV TPRERIVQAM EEIKEELAAR RKVLLENNKL LEEQRLTQRT QFDLEMMNEL 310 320 330 340 350 360 GYCSGIENYS RFLSGRGPGE PPPTLFDYLP ADGLLVVDES HVTIPQIGGM YRGDRARKET 370 380 390 400 410 420 LVEYGFRLPS ALDNRPLKFE EFEALAPQTI YVSATPGNYE LEKSGGDVVD QVVRPTGLLD 430 440 450 460 470 480 PIIEVRPVAT QVDDLLSEIR QRAAINERVL VTTLTKRMAE DLTEYLEEHG ERVRYLHSDI 490 500 510 520 530 540 DTVERMEIIR DLRLGEFDVL VGINLLREGL DMPEVSLVAI LDADKEGFLR SERSLIQTIG 550 560 570 580 590 600 RAARNVNGKA ILYGDKITPS MAKAIGETER RREKQQKYNE EHGITPQGLN KKVVDILALG 610 620 630 640 650 660 QNIAKTKAKG RGKSRPIVEP DNVPMDMSPK ALQQKIHELE GLMMQHAQNL EFEEAAQIRD 670 QLHQLRELFI AAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequences of the E. coli uvrB gene and protein." Arikan E., Kulkarni M.S., Thomas D.C., Sancar A. Nucleic Acids Res. 14:2637-2650(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, PROTEOLYTIC PRODUCT. Strain: K12.
[2]	"Structure of the uvrB gene of Escherichia coli. Homology with other DNA repair enzymes and characterization of the uvrB5 mutation." Backendorf C., Spaik H., Barbeiro A.P., van de Putte P. Nucleic Acids Res. 14:2877-2890(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 168-673. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[7]	"The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands." Verhoeven E.E., Wyman C., Moolenaar G.F., Goosen N. EMBO J. 21:4196-4205(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DIMERIC STATE OF UVRB.
[8]	"Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction." Sohi M., Alexandrovich A., Moolenaar G., Visse R., Goosen N., Vernede X., Fontecilla-Camps J.-C., Champness J., Sanderson M.R. FEBS Lett. 465:161-164(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 619-673.
[9]	"NMR assignments and secondary structure of the UvrC binding domain of UvrB." Alexandrovich A., Sanderson M.R., Moolenaar G.F., Goosen N., Lane A.N. FEBS Lett. 451:181-185(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 619-673.
[10]	"Clue to damage recognition by UvrB: residues in the beta-hairpin structure prevent binding to non-damaged DNA." Moolenaar G.F., Hoeglund L., Goosen N. EMBO J. 20:6140-6149(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF 95-TYR-TYR-96; TYR-101 AND PHE-108.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03678 Genomic DNA. Translation: CAA27314.1.
X03722 Genomic DNA. Translation: CAA27357.1.
U00096 Genomic DNA. Translation: AAC73866.1.
AP009048 Genomic DNA. Translation: BAA35437.2.

PIR

BVECUB. A93613.

RefSeq

NP_415300.1. NC_000913.2.
YP_489052.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E52	NMR	-	A/B	619-673	[»]
1QOJ	X-ray	3.00	A/B	619-673	[»]

ProteinModelPortal

P0A8F8.

SMR

P0A8F8. Positions 5-596, 627-672.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48012N.

IntAct

P0A8F8. 11 interactions.

MINT

MINT-1244062.

STRING

511145.b0779.

Proteomic databases

PaxDb

P0A8F8.

PRIDE

P0A8F8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73866; AAC73866; b0779.
BAA35437; BAA35437; BAA35437.

GeneID

12930963.
945385.

KEGG

ecj:Y75_p0752.
eco:b0779.

PATRIC

32116759. VBIEscCol129921_0805.

Organism-specific databases

EchoBASE

EB1055.

EcoGene

EG11062. uvrB.

Phylogenomic databases

eggNOG

COG0556.

HOGENOM

HOG000073580.

KO

K03702.

OMA

CIYGLGI.

ProtClustDB

PRK05298.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11062-MONOMER.
ECOL316407:JW0762-MONOMER.
MetaCyc:EG11062-MONOMER.

Gene expression databases

Genevestigator

P0A8F8.

Family and domain databases

Gene3D

4.10.860.10. 1 hit.

HAMAP

MF_00204. UvrB.

InterPro

IPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR001943. UVR_dom.
IPR004807. UvrB.
IPR024759. UvrB_YAD/RRR_dom.
[Graphical view]

PANTHER

PTHR24029. PTHR24029. 1 hit.

Pfam

PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF02151. UVR. 1 hit.
PF12344. UvrB. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

SUPFAM

SSF46600. UvrB_C. 1 hit.

TIGRFAMs

TIGR00631. uvrb. 1 hit.

PROSITE

PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50151. UVR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A8F8.

Entry information

Entry name

UVRB_ECOLI

Accession

Primary (citable) accession number: P0A8F8
Secondary accession number(s): P07025

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program