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Database: UniProt
Entry: Q65ST2
LinkDB: Q65ST2
Original site: Q65ST2 
ID   UVRB_MANSM              Reviewed;         678 AA.
AC   Q65ST2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 94.
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=MS1371;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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}.
DR   EMBL; AE016827; AAU37978.1; -; Genomic_DNA.
DR   RefSeq; WP_011200545.1; NC_006300.1.
DR   SMR; Q65ST2; -.
DR   STRING; 221988.MS1371; -.
DR   PRIDE; Q65ST2; -.
DR   EnsemblBacteria; AAU37978; AAU37978; MS1371.
DR   KEGG; msu:MS1371; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   BioCyc; MSUC221988:MS_RS06275-MONOMER; -.
DR   Proteomes; UP000000607; 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; 1.
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..678
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_0000227327"
FT   DOMAIN          31..417
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          436..602
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          638..673
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   NP_BIND         44..51
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   MOTIF           97..120
FT                   /note="Beta-hairpin"
SQ   SEQUENCE   678 AA;  77429 MW;  288FCAE70CA1C3AC CRC64;
     MSHKINSKPF ILHSEFKPSG DQPQAIEILA ENLNDGLAHQ TLLGVTGSGK TFTIANVIAK
     LNRPAMLLAP NKTLAAQLYA EMKAFFPENA VEYFVSYYDY YQPEAYVPSS DTFIEKDASI
     NDQIEQMRLS ATKSFLERRD TIVVASVSAI YGLGDPDSYL KMMLHLQTGA IIDQRQILVR
     LAELQYTRND QAFQRGTFRV RGEIIDIFPA ESDDRAVRIE LFDDEIERLS LFDPLTGTGF
     GAVPRFTVYP KTHYVTPREQ ILDAIEKIKS ELADRREYFI KENKLLEEQR ITQRTQFDIE
     MMNELGYCSG IENYSRYLSG RNEGEPPPTL FDYMPSDALL VIDESHVTVP QIGGMYRGDR
     SRKETLVEYG FRLPSALDNR PLRFEEFERL APQTIYVSAT PGPYELEKSG TEIIDQVVRP
     TGLLDPEIEI RPVSIQVDDL LSEARQRADR NERVLVTTLT KRMAEDLTDY LDEHGIRVRY
     LHSDIDTVER VEIIRDLRLG EFDVLVGINL LREGLDIPEV SLVAILDADK EGFLRSERSL
     IQTIGRAARN LKGKAILYAD RITNSMEKAI TETNRRREKQ MKYNEEHGIT PQGLNKKVGE
     LLDIGQGGSN KSRNKPRSQK AAEPATTYAI PMTAKEYQQQ IKKLEQQMYK FAQDLEFEKA
     AAIRDQLHKL REQFVENG
//
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