ID G0EPA3_BRAIP Unreviewed; 682 AA.
AC G0EPA3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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:AEM21973.1};
GN OrderedLocusNames=Bint_1354 {ECO:0000313|EMBL:AEM21973.1};
OS Brachyspira intermedia (strain ATCC 51140 / PWS/A) (Serpulina intermedia).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=1045858 {ECO:0000313|EMBL:AEM21973.1, ECO:0000313|Proteomes:UP000008522};
RN [1] {ECO:0000313|EMBL:AEM21973.1, ECO:0000313|Proteomes:UP000008522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51140 / PWS/A {ECO:0000313|Proteomes:UP000008522};
RX PubMed=21816042; DOI=10.1186/1471-2164-12-395;
RA Hafstrom T., Jansson D.S., Segerman B.;
RT "Complete genome sequence of Brachyspira intermedia reveals unique genomic
RT features in Brachyspira species and phage-mediated horizontal gene
RT transfer.";
RL BMC Genomics 12:395-395(2011).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00204}.
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DR EMBL; CP002874; AEM21973.1; -; Genomic_DNA.
DR RefSeq; WP_014487802.1; NC_017243.1.
DR AlphaFoldDB; G0EPA3; -.
DR KEGG; bip:Bint_1354; -.
DR PATRIC; fig|1045858.4.peg.1352; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_12; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000008522; 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; 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}; 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};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 24..155
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 427..593
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 625..660
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 656..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 90..113
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 682 AA; 78909 MW; CA2EFC6618D92773 CRC64;
MNFKLESNFK PSGDQVTAID SLVKGLENKN KYQTLLGVTA SGKTFTIANV IEKANRPTLV
MSHNKTLAAQ LYRELKDFFP NNAVEYFVSY YDYYQPEAYV PAKDLYIDKD ASVNDEIDRL
RLKATTSLLE RRDVIIVASV SCIYGLGSPE DYRKLYIAIE KDGEYDRDEI IEKLVSIQYE
RVKDVLERAR FKVIGDTIEI MSAYSDEVIR VEFFGDTVER IIKINPITRQ KLAEQDRVVI
YPAKHFVTGG DKLATGIKLI EEELEEQYNK FKSEGKLVEA ERIYGRTKYD LEMLREVGYC
AGIENYSRPL SGRKEGDRPA CLIDYFPDDF LTIIDESHVS VPQIRGMFFG DRSRKETLVK
YGFRLPSALD NRPLYFEEFE KLTHDTIYIS ATPAEYELKK SSQVVEQIIR PTGLLDPIIE
VYPIDGQIDR ILEEIKKTVS NNERIFITTL TKKMAEDLTK YLNENGVRTR YLHSDIQTVE
RVEIIRDLRL GAFDVLVGIN LLREGLDVPE VSLILILDAD KTGFLRNTTT LIQTIGRAAR
NANGRVIMFA DSISDAMKVA IDETERRRKI QMEYNKEHNI TPKTIIKKIQ DIIEREEKVE
TSYELHFDFR RFNERVKIDP EQKSDDYIKE LEKEMKKASD SLEFEKAIEI REKINQLKQL
KPQKKNVHKN VTSKNPNGKT NK
//
