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Database: UniProt
Entry: Q9PPM7
LinkDB: Q9PPM7
Original site: Q9PPM7 
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   31-JUL-2019, entry version 116.
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};
GN   OrderedLocusNames=Cj0680c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 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.,
RA   Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA   Whitehead S., 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
CC       of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon
CC       binding of the UvrA(2)B(2) complex to a putative damaged site, the
CC       DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP
CC       binding by UvrB and probably causes local melting of the DNA
CC       helix, facilitating insertion of UvrB beta-hairpin between the DNA
CC       strands. Then UvrB probes one DNA strand for the presence of a
CC       lesion. If a lesion is found the UvrA subunits dissociate and the
CC       UvrB-DNA preincision complex is formed. This complex is
CC       subsequently bound by UvrC and the second UvrB is released. If no
CC       lesion is found, the DNA wraps around the other UvrB subunit that
CC       will check the other stand for damage. {ECO:0000255|HAMAP-
CC       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}.
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   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; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   BioCyc; CJEJ192222:G1G1F-654-MONOMER; -.
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:ATPase 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   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; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW   DNA repair; Excision nuclease; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   CHAIN         1    657       UvrABC system protein B.
FT                                /FTId=PRO_0000138383.
FT   DOMAIN       23    414       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      431    593       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      622    657       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      36     43       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        89    112       Beta-hairpin.
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
//
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