ID A0A150MLR4_9BACI Unreviewed; 673 AA.
AC A0A150MLR4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=B4113_1835 {ECO:0000313|EMBL:KYD25428.1};
OS Geobacillus sp. B4113_201601.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1586290 {ECO:0000313|EMBL:KYD25428.1, ECO:0000313|Proteomes:UP000075654};
RN [1] {ECO:0000313|EMBL:KYD25428.1, ECO:0000313|Proteomes:UP000075654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4113_201601 {ECO:0000313|EMBL:KYD25428.1,
RC ECO:0000313|Proteomes:UP000075654};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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: 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:KYD25428.1}.
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DR EMBL; LQYX01000094; KYD25428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150MLR4; -.
DR PATRIC; fig|1586290.3.peg.1907; -.
DR Proteomes; UP000075654; 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};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 41..175
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 445..611
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 637..672
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 268..299
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 629..660
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 107..130
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 673 AA; 77061 MW; 2F62DDEE57595446 CRC64;
MWYNGERWYG EGGGTVEGRF QLVSSYQPQG DQPQAIAKLV DGLRQGVKHQ TLLGATGTGK
TFTISNVIAQ VNKPTLVIAH NKTLAGQLYS ELKEFFPHNA VEYFVSYYDY YQPEAYVPQT
DTYIEKDAKI NDEIDKLRHS ATSALFERRD VIIVASVSCI YGLGSPEEYR ELVVSLRVGM
EIERNALLRR LVDIQYDRND IDFRRGTFRV RGDVVEIFPA SRDEHCIRVE FFGDEIDRIR
EVDALTGEVL GEREHVAIFP ASHFVTREEK MRLAIQNIEQ ELEERLAELR AQGKLLEAQR
LEQRTRYDLE MMREMGFCSG IENYSRHLAL RPPGSTPYTL LDYFPDDFLI IIDESHVTLP
QLRGMYNGDR ARKQVLVDHG FRLPSALDNR PLTFEEFEQK IKQIIYVSAT PGPYELEHSP
GVVEQIIRPT GLLDPTIDVR PTNGQIDDLI GEIRERVERN ERTLVTTLTK KMAEDLTDYL
KEAGIKVAYL HSEIKTLERI EIIRDLRLGK YDVLVGINLL REGLDIPEVS LVAILDADKE
GFLRSERSLI QTIGRAARNA NGHVIMYADT VTKSMEIAIQ ETKRRRTIQE AYNQEHGIVP
RTVKKEIRDV IRATYAAEET ETYEAKAPAK MTKQEREELI RTLEAEMKAA AKALDFERAA
QLRDAIFELK AEG
//
