UVRB_CAMJE
ID UVRB_CAMJE Reviewed; 657 AA.
AC Q9PPM7; Q0PAJ9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204};
DE Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204};
DE AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204};
GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; OrderedLocusNames=Cj0680c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. A damage recognition complex composed of 2
CC UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of
CC the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps
CC around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB
CC and probably causes local melting of the DNA helix, facilitating
CC insertion of UvrB beta-hairpin between the DNA strands. Then UvrB
CC probes one DNA strand for the presence of a lesion. If a lesion is
CC found the UvrA subunits dissociate and the UvrB-DNA preincision complex
CC is formed. This complex is subsequently bound by UvrC and the second
CC UvrB is released. If no lesion is found, the DNA wraps around the other
CC UvrB subunit that will check the other stand for damage.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP-
CC Rule:MF_00204}.
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DR EMBL; AL111168; CAL34817.1; -; Genomic_DNA.
DR PIR; C81338; C81338.
DR RefSeq; WP_002855027.1; NC_002163.1.
DR RefSeq; YP_002344098.1; NC_002163.1.
DR AlphaFoldDB; Q9PPM7; -.
DR SMR; Q9PPM7; -.
DR IntAct; Q9PPM7; 7.
DR STRING; 192222.Cj0680c; -.
DR PaxDb; Q9PPM7; -.
DR PRIDE; Q9PPM7; -.
DR EnsemblBacteria; CAL34817; CAL34817; Cj0680c.
DR GeneID; 904998; -.
DR KEGG; cje:Cj0680c; -.
DR PATRIC; fig|192222.6.peg.672; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_7; -.
DR OMA; EYVDRMV; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_00204; UvrB; 1.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR036876; UVR_dom_sf.
DR InterPro; IPR004807; UvrB.
DR InterPro; IPR041471; UvrB_inter.
DR InterPro; IPR024759; UvrB_YAD/RRR_dom.
DR PANTHER; PTHR24029; PTHR24029; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF12344; UvrB; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46600; SSF46600; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00631; uvrb; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..657
FT /note="UvrABC system protein B"
FT /id="PRO_0000138383"
FT DOMAIN 23..414
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 431..593
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 622..657
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 89..112
FT /note="Beta-hairpin"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 657 AA; 75936 MW; 74E2B4892C9FAD09 CRC64;
MLELTSEFKP SPDQQEAIKG IVKSIKKGNK YQTLLGVTGS GKTFTMANVI KELNIPTLIM
SHNKSLCAQL YSEFKGFFSK NHVEYFISYY DYYQPEAYIP RTDVFIEKDS STNEDLERLR
LSATASLLSY EDVVCIASVS ANYGLGNPNE YIGMVLIFEL GMQISQKELL KKLVDMGYKR
NDNFFDRADF RVQGDIIDIY PAYYEDEVVR LEFFGDELDA MYHYNVLENK KGKDLKRFIL
YPTSQFSVGE TRLKQAIKDI KAELNERLAY FEHENKLVEY QRLKQRVEFD LEMLTSTGMC
KGVENYARHL TGLKEGDTPY TLFDYFAIKD RKFLVIVDES HVSLPQFRGM FAGDRSRKQT
LVDYGFRLPS ALDNRPLMFD EFIHKNCQFL FVSATPAPLE LELSKENIFH QIMRPTGLLD
PLIELKDSDN QVEILFDEAK KVIQRNERVL VTVLTKKLAE ELTRYYLELG IKVKYMHSDI
DAIERNEIIR GLRSGAFDML IGINLLREGL DLPEVSLIAI MDADKEGFLR STTSLIQTMG
RAARNVNGKV LLFCKKITKS MQEAMDTTNE RRKLQMAYNK KYNITPTSVK RHIEESLKNE
EDLGEIYRKG KKLEKMPASE RAKLVKELRK QMLEAAKALE FEKAAAIRDE INKLRDL
