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UVRB_CLOTE
ID   UVRB_CLOTE              Reviewed;         661 AA.
AC   Q890X8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=CTC_02504;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO36967.1; -; Genomic_DNA.
DR   RefSeq; WP_011100628.1; NC_004557.1.
DR   AlphaFoldDB; Q890X8; -.
DR   SMR; Q890X8; -.
DR   STRING; 212717.CTC_02504; -.
DR   PRIDE; Q890X8; -.
DR   EnsemblBacteria; AAO36967; AAO36967; CTC_02504.
DR   GeneID; 64180041; -.
DR   KEGG; ctc:CTC_02504; -.
DR   HOGENOM; CLU_009621_2_1_9; -.
DR   OMA; EYVDRMV; -.
DR   OrthoDB; 95696at2; -.
DR   Proteomes; UP000001412; 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; 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..661
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_0000227303"
FT   DOMAIN          25..412
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          429..595
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           91..114
FT                   /note="Beta-hairpin"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   661 AA;  76050 MW;  93681663825757FF CRC64;
     MEKLKVHSKF EPKGDQPKAI RSISDGILKG DKYQTLLGVT GSGKTFTMAK IIEQVQKPTL
     VLAHNKTLAA QLCSEFREFF PENSVEYFVS YYDYYQPEAY VAQTDTYIEK DASINDEIDK
     LRHSATSALL ERKDVIIVSS VSCIYGLGNP EEYKNLTISL REGMEKDRDE ILKKLVEIQY
     ERNEINFVRG TFRVRGDVLD IFPASSSNIA IRVEFFGDEI EKIREFDSLT GEIVGKRNHV
     SIFPASHFAT SKERLEVGIK KIEEELEIRV QEFIKEDKLL EAQRIKQRTN FDIEMMRELG
     YCSGIENYSR ILDGRAAGTP PQTLLDYFPE DFLLFVDESH VTLPQVRGMY GGDRSRKDNL
     VNYGFRLPSA YDNRPLKFNE FQSKLNRVVF VSATPGDHEL DKSSNVAEQI IRPTGLLDPE
     IIVKPIKGQI DDLYSNINET IKNGFRVLVT TLTKKMAEDL TEYFKEMNIK TRYLHSDIDT
     IERMKIIREL RLGEFDVLVG INLLREGLDI PEVALVAILD ADKEGFLRSD RSLIQIIGRA
     ARNSESKVIM YADNITKSMD RAIKETNRRR VIQMEYNKEN NIVPQTIIKD IREVIEATKV
     VEEEAEYDSL EEAIQANNEN LEELISKYEA DMRKAAKELE FEKAAHYRDI IQKLKKQLSN
     I
 
 
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