ID T0Z6R0_9BACT Unreviewed; 692 AA.
AC T0Z6R0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=D084_Lepto4C00373G0005 {ECO:0000313|EMBL:EQD24709.1};
OS Leptospirillum sp. Group IV 'UBA BS'.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1260983 {ECO:0000313|EMBL:EQD24709.1, ECO:0000313|Proteomes:UP000017751};
RN [1] {ECO:0000313|EMBL:EQD24709.1, ECO:0000313|Proteomes:UP000017751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23645189; DOI=10.1128/AEM.00202-13;
RA Goltsman D.S., Dasari M., Thomas B.C., Shah M.B., VerBerkmoes N.C.,
RA Hettich R.L., Banfield J.F.;
RT "New group in the Leptospirillum clade: cultivation-independent community
RT genomics, proteomics, and transcriptomics of the new species
RT "Leptospirillum group IV UBA BS".";
RL Appl. Environ. Microbiol. 79:5384-5393(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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00204}.
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}.
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:EQD24709.1}.
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DR EMBL; AURA01000373; EQD24709.1; -; Genomic_DNA.
DR AlphaFoldDB; T0Z6R0; -.
DR PATRIC; fig|1260983.3.peg.965; -.
DR HOGENOM; CLU_009621_2_1_0; -.
DR Proteomes; UP000017751; 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 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000017751};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204}.
FT DOMAIN 40..171
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 445..607
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 640..671
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 672..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 692 AA; 77835 MW; C8210892990CA1F4 CRC64;
MTGSPGGGEA LVPVRSGRFE LVSGYAPCGD QGQAIEILSE GVRKGASRQT LLGVTGSGKT
FTMANVIANS GKPALVLAPN KTLAAQLYRE FKEFFPNNRV EYFVSYYDYY QPEAYLPATD
TYIEKDSAVN DLIDRMRHSA TSALLERLDT IVVASVSCIY GLGSPDSYLK MHLYLERGME
IRRNRLLERL VEIQYQRNEI DFHRGTFRVK GDVVDIFPAS FEDRAVRVEF WGDTIEKIRE
IDPLTGHELL QVPSMIIYPG THYVLPPDQL EGALAGIEEE LHERIAWFRK NNQLVEAQRI
EQRTLFDLEM IREVGFCHGI ENYSRHLSGR APGEPPPTLF DYFPRDFLLV IDESHVAIPQ
VGGMYHGDHS RKKSLVEYGF RLPSAFDNRP LTFSEFEQVM RQVIFVSATP GPYELAASGG
VTAEQVIRPT GLLDPEIEVV PALHQVDHLL GEVRRTVAQG DRVLVTTLTK RMAENLTEYL
DERGVRVRYL HSEIDTLERM EIIRNLRRGE FDVLVGINLL REGLDLPEVS LVAILDADRE
GFLRSRRSLI QTSGRAARNL RGRVVFYGDT VTGSMQEAID ETRRRRAIQI AFNEKNGIVP
RGIQKSIPEA LYHVSEGDYV TVPVSEEAGA TGPEASLPEE EIRRRMVAAA EDLDFEMAAH
YRDLLRARGE KPSGEGIVLK ASRGGGRRKK GR
//
