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Database: UniProt
Entry: UVRB_THIDA
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ID   UVRB_THIDA              Reviewed;         675 AA.
AC   Q3SIK7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=Tbd_1568;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97521.1; -; Genomic_DNA.
DR   RefSeq; WP_011312080.1; NC_007404.1.
DR   AlphaFoldDB; Q3SIK7; -.
DR   SMR; Q3SIK7; -.
DR   STRING; 292415.Tbd_1568; -.
DR   KEGG; tbd:Tbd_1568; -.
DR   eggNOG; COG0556; Bacteria.
DR   HOGENOM; CLU_009621_2_1_4; -.
DR   OrthoDB; 9806651at2; -.
DR   Proteomes; UP000008291; 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   CDD; cd17916; DEXHc_UvrB; 1.
DR   CDD; cd18790; SF2_C_UvrB; 1.
DR   Gene3D; 6.10.140.240; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
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   NCBIfam; TIGR00631; uvrb; 1.
DR   PANTHER; PTHR24029; UVRABC SYSTEM PROTEIN B; 1.
DR   PANTHER; PTHR24029:SF0; UVRABC SYSTEM PROTEIN B; 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; C-terminal UvrC-binding domain of UvrB; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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..675
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_0000227378"
FT   DOMAIN          31..419
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          435..601
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          632..667
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   MOTIF           97..120
FT                   /note="Beta-hairpin"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   675 AA;  76862 MW;  54D65913FD5D41D2 CRC64;
     MFVTFPDSPF RLFQPFPPAG DQPTAIARLI EGIDDGLSYQ TLLGVTGSGK TYTMANVIAR
     AGRPALIMAP NKTLAAQLYA EMREFFPENA VEYFVSYYDY YQPEAYVPAR DLFIEKDSSI
     NEHIEQMRLS ATKSLLERRD TVIVCTVSAI YGIGDPSDYH SMILLLRQND KMTQREVIAR
     LTQMQYDRND VDFKRGVFRV RGDVIDIFPA EHAETAIRVE LFDDVVETLH LFDPLTGQIL
     QKVSRFTVFP SSHYVTPRET TLRAIEAIKV ELRERLDWYY ANNKLVEAQR LEQRTRFDLE
     MMVELGFCKG IENYSRHLSG RKAGEPPPTL IDYLAKDALM FIDESHVTVT QVGGMYKGDR
     SRKENLVDYG FRLPSALDNR PLKFEEFEAL MPQTVFVSAT PAKYEAEHAG QVVEQLVRPT
     GLIDPIVEVR PVTTQVDDLM SEVKKRVAVG ERVLVTTLTK RMAEDLTDYL AEHGVKVRYL
     HSDIDTVERV EIIRDLRLGE FDVLVGINLL REGLDIPEVS LVAILDADKE GFLRSERSLI
     QTIGRAARHL NGTAILYADR ITDSMQRAIG ETERRRAKQI AFNTEHGITP RGVVKRIKDI
     IDGVYDADAS RQELKAAQTA AEYKVMDEKS LTKRVKKIEK EMQDAAKNLE FEKAAVLRDQ
     LKELKALLFG VEERE
//
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