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Entry: F7UZ70_EEGSY
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ID   F7UZ70_EEGSY            Unreviewed;       716 AA.
AC   F7UZ70;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=UvrABC system protein B {ECO:0000256|ARBA:ARBA00029504, ECO:0000256|HAMAP-Rule:MF_00204};
DE            Short=Protein UvrB {ECO:0000256|HAMAP-Rule:MF_00204};
DE   AltName: Full=Excinuclease ABC subunit B {ECO:0000256|HAMAP-Rule:MF_00204};
GN   Name=UvrB {ECO:0000313|EMBL:BAK43813.1};
GN   Synonyms=uvrB {ECO:0000256|HAMAP-Rule:MF_00204};
GN   OrderedLocusNames=EGYY_06000 {ECO:0000313|EMBL:BAK43813.1};
OS   Eggerthella sp. (strain YY7918).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Eggerthella.
OX   NCBI_TaxID=502558 {ECO:0000313|EMBL:BAK43813.1, ECO:0000313|Proteomes:UP000008929};
RN   [1] {ECO:0000313|EMBL:BAK43813.1, ECO:0000313|Proteomes:UP000008929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YY7918 {ECO:0000313|EMBL:BAK43813.1,
RC   ECO:0000313|Proteomes:UP000008929};
RX   PubMed=21914883;
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete Genomic Sequence of the Equol-Producing Bacterium Eggerthella sp.
RT   Strain YY7918, Isolated from Adult Human Intestine.";
RL   J. Bacteriol. 193:5570-5571(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YY7918 {ECO:0000313|Proteomes:UP000008929};
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete genome sequence of the equol-producing bacterium Eggerthella sp.
RT   strain YY7918 isolated from adult human intestine.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00026033, ECO:0000256|HAMAP-Rule:MF_00204,
CC       ECO:0000256|RuleBase:RU003587}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587}.
CC   -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00204}.
CC   -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000256|ARBA:ARBA00008533,
CC       ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587}.
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DR   EMBL; AP012211; BAK43813.1; -; Genomic_DNA.
DR   RefSeq; WP_013979063.1; NC_015738.1.
DR   AlphaFoldDB; F7UZ70; -.
DR   STRING; 502558.EGYY_06000; -.
DR   KEGG; eyy:EGYY_06000; -.
DR   eggNOG; COG0556; Bacteria.
DR   HOGENOM; CLU_009621_2_1_11; -.
DR   OrthoDB; 9806651at2; -.
DR   Proteomes; UP000008929; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00204}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00204};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW   Rule:MF_00204};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00204};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW   Rule:MF_00204}; Helicase {ECO:0000313|EMBL:BAK43813.1};
KW   Hydrolase {ECO:0000313|EMBL:BAK43813.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00204}; Reference proteome {ECO:0000313|Proteomes:UP000008929};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587}.
FT   DOMAIN          47..172
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          450..616
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          644..679
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          689..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          640..667
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           113..136
FT                   /note="Beta-hairpin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   716 AA;  81301 MW;  81487440E8E26EAD CRC64;
     MAHLSNIDGI EMEGKLPDVR LANTPFKVVS PYEPSGDQPQ AIKQLAHGVD EGLRYQTLLG
     VTGSGKTFTM AKTIEAVQKP TLVMAPNKTL AAQLASELKE FFPDNSVVYF VSYYDYYQPE
     AYVPSSDTFI EKDASINEEV EKLRHAATSA LLSRRDCIVV ASVSCIYGIG SPMDYAGMAV
     FVDKQKEMDR DDVIHELIDI QYDRNDYELK RGTFRVRGDS LDVFPPYADN PVRIDFWGDE
     IEGITEIDHV TGEVINEFEA LPIWPASHYV TARPKMDRAL GTIRDELRER LQQFKEEGKL
     LEAQRLEMRV NYDLEMLETM GFCSGIENYS RHMDGREPGE PPYTLIDYFP KDFLCIIDES
     HVTVPQIRGM HEGDRSRKIT LAEHGFRLPS CLDNRPLRFD EFESRVPQFI YVSATPGDYE
     QKVSQQQVEQ IIRPTGLLDP EIIVRGSASQ IDDIIDEAKE RAARDERVLI TTLTKKMAED
     LTDHLLDQGV KARYMHSDIA TLERVEILRE LRQGKFDVLV GINLLREGLD LPEVSLVAIL
     DADKEGFLRN HRSLIQTIGR AARNVSGQVI MYADKTTDSM DLAINETRRR RAIQMQYNEE
     HGIEPQTIRK AINDIMSYVT DEMGNTTAEQ VNKELAELSR EEVLRIIQSM EDDMADASRN
     MDFEEAARLR DQVVKLRVQV EGGSEEDVLK DLKKGARKGS AFGNRKNSAY GSSRRS
//
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