ID T0BQF2_ALIAG Unreviewed; 663 AA.
AC T0BQF2; A0A9E6ZG89;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:UNO49770.1};
GN ORFNames=K1I37_04470 {ECO:0000313|EMBL:UNO49770.1};
OS Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS / NCIMB 13137 / GD3B).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1356854 {ECO:0000313|EMBL:UNO49770.1, ECO:0000313|Proteomes:UP000829401};
RN [1] {ECO:0000313|Proteomes:UP000829401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3922 {ECO:0000313|Proteomes:UP000829401};
RX PubMed=36240455; DOI=10.1093/g3journal/jkac225;
RA Leonardo I.C., Barreto Crespo M.T., Gaspar F.B.;
RT "Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris
RT DSM 3922T, a taint-producing strain.";
RL G3 (Bethesda) 12:0-0(2022).
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; CP080467; UNO49770.1; -; Genomic_DNA.
DR RefSeq; WP_021297831.1; NZ_AURB01000164.1.
DR STRING; 1356854.N007_01150; -.
DR KEGG; aaco:K1I37_04470; -.
DR Proteomes; UP000829401; 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; 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}; 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}; Hydrolase {ECO:0000313|EMBL:UNO49770.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00204}; Reference proteome {ECO:0000313|Proteomes:UP000829401};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT MOTIF 95..118
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 663 AA; 75128 MW; C0E5894B475BF510 CRC64;
MATQPGKFEL VSEYKPQGDQ PAAIDALVDG VESGLRHQTL LGVTGSGKTF TMANIIQEVN
RPTLVIAHNK TLAAQLAAEF REFFPNNAVE YFVSYYDYYQ PEAYIPSTDT FIEKDAKIND
EIDKLRHSAT AALLERNDVI VVASVSAIYG LGSPAEYSQH VLSLRVGATM DRNQILRRLV
DMQYERNDIN FTRGTFRVRG DVVEIFPASR DENAIRVELF GDEIDRITEI HVVTGQVVAR
RNHVSIFPAS HFVTSRPRLE MAISRIKEEL RERLAELRDD GKLLEAQRLE QRTMYDIEMM
LEIGFCSGIE NYSRHLEGRA AGEPPNTLLD YFPPGFLTLI DESHVTLPQI RGMYGGDRSR
KETLIEHGFR LPSAADNRPL TFEEFERAVG QCIYVSATPG PYEEEHQQRI VEQIIRPTGL
LDPTISVRPI KGQIDDLVGE IRARIRNDER VLVTTLTKKM AEDLTDYLKE IGIRVRYLHS
DIKTIERMVI LRDLRKGAFD VLVGINLLRE GLDLPEVSLV AILDADKEGF LRAHRSLIQT
IGRAARNANG AVIMYADKIT DSMRIAIDET ERRRAKQIAY NEEHGITPTT IRKAVRDVIE
STKVAEETED YVSVAEQAQQ LSKRERKELV AKLEAEMREA AKELQFERAA QLRDMISELT
NAS
//
