ID W0SE51_9PROT Unreviewed; 690 AA.
AC W0SE51;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
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 ORFNames=SUTH_01707 {ECO:0000313|EMBL:BAO29499.1};
OS Sulfuritalea hydrogenivorans sk43H.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Sulfuritalea.
OX NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO29499.1, ECO:0000313|Proteomes:UP000031637};
RN [1] {ECO:0000313|EMBL:BAO29499.1, ECO:0000313|Proteomes:UP000031637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM22779 {ECO:0000313|EMBL:BAO29499.1};
RX PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010;
RA Watanabe T., Kojima H., Fukui M.;
RT "Complete genomes of freshwater sulfur oxidizers Sulfuricella denitrificans
RT skB26 and Sulfuritalea hydrogenivorans sk43H: genetic insights into the
RT sulfur oxidation pathway of betaproteobacteria.";
RL Syst. Appl. Microbiol. 37:387-395(2014).
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; AP012547; BAO29499.1; -; Genomic_DNA.
DR AlphaFoldDB; W0SE51; -.
DR STRING; 1223802.SUTH_01707; -.
DR KEGG; shd:SUTH_01707; -.
DR HOGENOM; CLU_009621_2_1_4; -.
DR Proteomes; UP000031637; 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; 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:UP000031637};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00204}.
FT DOMAIN 40..173
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 444..610
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 641..676
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 271..298
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 637..664
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 106..129
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 690 AA; 78315 MW; 29FBDFF4DC62AC64 CRC64;
MAEIHELKGR VVEFPGSPWR LHQPFPPAGD QPEAIRLLTE GIADGLSFQT LLGVTGSGKT
YTMANVIARL GRPALVLAPN KTLAAQLYSE FREFFPENAV EYFVSYYDYY QPEAYVPSRD
LFIEKDSSIN EHIEQMRLSA TKSLLERRDV VIVCTVSAIY GIGDPVDYHS MILHLRTGEK
IGQREVIRRL TEMQYERNEM DFKRGVYRVR GDVIDIFPAE NAESAVRITL FDDELESITL
FDPLTGHTRQ KLGRFTVFPS SHYVTPRATV LKAVEAIKAE LRQRIEFFQR EQKLVECQRI
EQRTRFDLEM LDQLGFCKGI ENYSRHLSGR QPGEPPPTLY DYLPNDAIMF VDESHVTIPQ
VGGMYKGDRS RKENLVDYGF RLPSALDNRP LKFDEFEKLM PQTVFVSATP AAYEEAHQGQ
VVEQLVRPTG LVDPVVEVRP ASTQVDDLLA ECKKRIAVGE RVLVTTLTKR LAEQLTEYLN
DNGIKVRYLH SDIDTVERVE IIRDLRLGEF DVLVGINLLR EGLDIPEVSL VAILDADKEG
FLRSTRSLIQ TMGRAARHLN GTAILYADRI TDSMQRAMGE TARRRAKQLA HNEAMGITPI
GVKKRIKDII DGVYDADTAV RELKAAQEAA RYEVMSEKDL SREIRRLEKA MQEHAKNLEF
EEAAAARDEL FRIQHLAFGG EAHDAPGDAV
//
