ID   A0A8J4WNQ1_9BACT        Unreviewed;       759 AA.
AC   A0A8J4WNQ1;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   02-OCT-2024, entry version 10.
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:0000256|HAMAP-Rule:MF_00204,
GN   ECO:0000313|EMBL:KAF5407919.1};
GN   ORFNames=Udaeo2_19440 {ECO:0000313|EMBL:KAF5407919.1};
OS   Candidatus Udaeobacter sp.
OC   Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC   Chthoniobacteraceae; Candidatus Udaeobacter.
OX   NCBI_TaxID=2665650 {ECO:0000313|EMBL:KAF5407919.1, ECO:0000313|Proteomes:UP000618171};
RN   [1] {ECO:0000313|EMBL:KAF5407919.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AEW3 {ECO:0000313|EMBL:KAF5407919.1};
RA   Willms I.M., Rudolph A.Y., Goeschel I., Bolz S.H., Schneider D., Penone C.,
RA   Poehlein A., Schoening I., Nacke H.;
RT   "Globally abundant Candidatus Udaeobacter benefits from release of
RT   antibiotics in soil.";
RL   Submitted (FEB-2020) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAF5407919.1}.
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DR   EMBL; JAALOD010000047; KAF5407919.1; -; Genomic_DNA.
DR   Proteomes; UP000618171; Unassembled WGS sequence.
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; 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-like.
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; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00204}; Reference proteome {ECO:0000313|Proteomes:UP000618171};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587}.
FT   DOMAIN          24..158
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          505..671
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          695..730
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          434..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          251..289
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           90..113
FT                   /note="Beta-hairpin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT   COMPBIAS        443..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..759
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   759 AA;  86268 MW;  AB5BDFBF1EF580A9 CRC64;
     MSFQLQSNYT PRGDQGQAIA KLIRSIEAGN RHQTLLGVTG SGKTFTIANV IRELDRPTLV
     ISHNKTLAAQ LYSEFKQFFP RNAVEYFVSY FDYYQPEAYI PRSDTYIEKD SSINEEIERL
     RLAATSALLS RRDTIVVASV SCIYGVTSPE DYLQMLLTIK RGQQVSREAV LSRLIEMLYD
     RNDVNFARGR FRVRGDVVEV YPGSADEEGI RIEFFGDEIE AITRFDPLTG HAHESLSVIT
     FYPAKQFVTP ADKLNRALRT IRDELEERII ELESQNKLLE AQRLRMRTEY DLEMLQEMGF
     CNGIENYSRH LSGRPPGSKP YTIIDFFPKD FLVVIDESHA TIPQIGGMYE GDRSRKTVLV
     NYGFRLPSAL DNRPLNFDEF MKLTNQLVYV SATPAEFEIQ NSVAGNKGYI PHRRQRIGEA
     ELVPFAVAGE KRSTPINREQ ALNSDKSRAR AQRSRSNSEV RVSRTDEPPE KFDVHTPGAQ
     LVVEQIIRPT GLLDPKITLK PLKNQIDETI ELCRQRVEKG ERVLVTTLTK RTAEDLADYL
     RDVGLKVRYL HSDIDAIERV EILRGLRAAD FDILVGINLL REGLDLPEVS LVCILDADKE
     GFLRSETSLI QTAGRAARHV NGEVVLFADQ VTRSMEALMS ISEYRRAKQL EYNEKHGITP
     QTVRRAVQES LHTILRGREI AASVIQEAGG DFNVTELLRE LEDEMQEASA NLEFERAALL
     RDQIMEVKSG TGISKIEPKR RPVKYSSRGR GTGRRRSRV
//