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Database: UniProt
Entry: B8KX86_9GAMM
LinkDB: B8KX86_9GAMM
Original site: B8KX86_9GAMM 
ID   B8KX86_9GAMM            Unreviewed;       673 AA.
AC   B8KX86;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 84.
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:EED34711.1};
GN   ORFNames=NOR51B_650 {ECO:0000313|EMBL:EED34711.1};
OS   Luminiphilus syltensis NOR5-1B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Luminiphilus.
OX   NCBI_TaxID=565045 {ECO:0000313|EMBL:EED34711.1, ECO:0000313|Proteomes:UP000004699};
RN   [1] {ECO:0000313|Proteomes:UP000004699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX   PubMed=23705883;
RA   Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT   "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT   OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT   syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT   Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT   halotolerans.";
RL   BMC Microbiol. 13:118-118(2013).
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; DS999411; EED34711.1; -; Genomic_DNA.
DR   RefSeq; WP_009019459.1; NZ_DS999411.1.
DR   AlphaFoldDB; B8KX86; -.
DR   STRING; 565045.NOR51B_650; -.
DR   eggNOG; COG0556; Bacteria.
DR   HOGENOM; CLU_009621_2_1_6; -.
DR   OrthoDB; 9806651at2; -.
DR   Proteomes; UP000004699; 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; 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 {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:UP000004699};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   Rule:MF_00204}.
FT   DOMAIN          26..183
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          430..583
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          634..669
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          637..669
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           92..115
FT                   /note="Beta-hairpin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   673 AA;  76424 MW;  7A43FFCB489EB5B8 CRC64;
     MSRQFEVKSN YQPAGDQPFA IQKLVDGINS GLAEQVLLGV TGSGKTFTMA NVVQQLQRPT
     IVMAHNKTLA AQLYGEFKEF FPNNAVEYFV SYYDYYQPEA YVPSSDTFIE KDAQVNDHIE
     QMRLSATKAL IEREDCLVVS TVSSIYGLGD PESYFKMVMH LSRGEIIDQR GILRQLAELQ
     YTRNDIDFKR GTYRVRGDVI DVFPADSDEL AIRIELFDEE IENLTTFDPL TGVIVEKLPR
     ITIFPKTHYV ASRDTMLGAI DLIEEELEGR VKQLKEADKL LEAQRIQQRT RYDIEMIREL
     GYCQGIENYS RYLSGRAPGE PPPTLFEYLP DNALIMVDES HVTVPQIGGM YKGDRSRKET
     LVEYGFRLPS ALDNRPLRFE EWEALRPQAI YVSATPGAYE TERSGQTVEQ VVRPTGLVDP
     EVEVRPARTQ VDDLLGEIHT TVAAGSRVLV TTLTKRMAED LTEYLSEHDI RVRYLHSDID
     TVERVEIIQD LRLGKFDVLV GINLLREGLD MPEVSLVAIL DADKEGFLRS DRSLIQTIGR
     AARHIDGRAI LYGDRMTGSM ERAIAETERR RVKQVEFNTE HGITPKGIEK SVQDILEGAR
     RMPTKPRSAR DRKVAEERAA YTAEVVNLSP KALARKLESM EAQMLEHAKN LEFEQAAQLR
     DQLTEIKQQA FVG
//
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