ID B9NR67_9RHOB Unreviewed; 728 AA.
AC B9NR67;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 87.
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:EEE38365.1};
GN ORFNames=RKLH11_2207 {ECO:0000313|EMBL:EEE38365.1};
OS Rhodobacteraceae bacterium KLH11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE38365.1, ECO:0000313|Proteomes:UP000005135};
RN [1] {ECO:0000313|Proteomes:UP000005135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX PubMed=21742885; DOI=10.1128/jb.05556-11;
RA Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL J. Bacteriol. 193:5011-5012(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}.
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DR EMBL; DS999531; EEE38365.1; -; Genomic_DNA.
DR AlphaFoldDB; B9NR67; -.
DR STRING; 467661.RKLH11_2207; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_5; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000005135; 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.
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:UP000005135};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00204}.
FT DOMAIN 49..202
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 454..620
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 647..682
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 697..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..670
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 115..138
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 728 AA; 82207 MW; 2A5C5FCEE9636A93 CRC64;
MAYAHSDKTQ LAADDVRARL KLEGGKSFVM HTEFAPAGDQ PTAITELAAG VHEGERDQVL
LGATGTGKTF TMAKVIEETQ RPAIILAPNK TLAAQLYGEF KGFFPENSVE YFVSYYDYYQ
PEAYVARSDT YIEKESQINE QIDRMRHSAT RALLERDDVI IVASVSCIYG IGSVETYGAM
TQDLKVGKEY DQRQVMADLV AQQYRRNDQA FQRGSFRVRG DSLEIWPAHL EDRAWKLSFF
GEELEQITEF DPLTGEKTDT MEHIRVYANS HYVTPKPTMQ QAIIGIKKEL RMRLDQLVGE
GKLLEAQRLE QRTNFDLEML EATGVCNGIE NYSRYLTGRA PGEPPPTLFE FIPDNAIVFA
DESHVSVPQI GGMYRGDYRR KFTLAEHGFR LPSCMDNRPL KFEEWDAMRP QSVFVSATPA
KWEIEQTGGI FTEQVIRPTG LLDPEVEIRP VSMQVDDLLD EVRKVAADGY RTLVTTLTKR
MAEDLTEYLH EQGIKVRYMH SDIDTLERIE ILRDLRLGAF DVLVGINLLR EGLDIPECGL
VAILDADKEG FLRSETSLVQ TIGRAARNAD GRVIMYADKI TGSMERALNE TNRRRAKQIA
YNEEHGITPE TVKKNVEDVL AGLYEGDVDM NRVTATIDKP MHGANLEAHL DGLREQMRKA
AENLEFEEAA NIRDEIKRLE AVDLAVADDP MARQWAVEKA SEDAVKSRGR STAGRPGQRG
GNVKRRKR
//
