UVRB_ANAMM
ID UVRB_ANAMM Reviewed; 651 AA.
AC Q5P9H3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204};
DE Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204};
DE AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204};
GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; OrderedLocusNames=AM1243;
OS Anaplasma marginale (strain St. Maries).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=234826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St. Maries;
RX PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT is skewed to two superfamilies of outer membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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:0000255|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:0000255|HAMAP-Rule:MF_00204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP-
CC Rule:MF_00204}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000030; AAV87057.1; -; Genomic_DNA.
DR RefSeq; WP_011114644.1; NZ_AFMU01000038.1.
DR AlphaFoldDB; Q5P9H3; -.
DR SMR; Q5P9H3; -.
DR KEGG; ama:AM1243; -.
DR HOGENOM; CLU_009621_2_1_5; -.
DR OMA; EYVDRMV; -.
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 Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR24029; PTHR24029; 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; SSF46600; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00631; uvrb; 1.
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; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Nucleotide-binding; SOS response.
FT CHAIN 1..651
FT /note="UvrABC system protein B"
FT /id="PRO_0000227277"
FT DOMAIN 25..411
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 427..591
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 616..651
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT REGION 593..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..114
FT /note="Beta-hairpin"
FT COMPBIAS 601..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 651 AA; 73824 MW; 7524D1C5C18BC2DE CRC64;
MQRFKISSEF NPSGDQPGAI DSLVRGISCG AKEQTLLGVT GSGKTFTMAS VIEQTQRPAI
IIAHNKTLAA QLHEEMRSFF PENAVEYFVS YYDYYQPEAY IPQSDVYIEK DALINDKIDL
LRHSATRSLL ERRDVVVVAS VSCIYGLGSP ELYSEMTVPI ALGMKLDMCQ LQERLVELQY
KHGNRYERGN FSVQGDVLSV FPSHYEDRIW KISFFGDEVD SIQEVDPKSG MVTLKLEKIK
IFPNSHYVTP RPTLLQAISE IEKELDECAL QFKQCNKIVE ADRIVERTRF DIEMMRETGT
CKGIENYSRY LCGKEAGDPP NTLLDYLPQD AIMFIDESHM TVPQIRAMYN GDRMRKANLI
NHGFRMPSAL DNRPLTFAEW EDRKPTVVYV SATPGQYELQ QTGGVATEQL IRPTGLLDPV
CIVKGADGQI HDVMCESQAT IARGYRVLIT TLTKKMAENL TEYMREMGIK VAYLHSDVKT
LERIEIISDL RLGVIDVLVG VNLMREGLDI PECALVGILD ADKEGFLRST TSLIQTIGRA
ARNVEGRVIL YANVITKSMR TAMEETDRRR DIQRKYNQEH SIVPRTIQKP VQTSLSERVG
SSRKKVSRDT NTDPANRDIV ELQKEMLLCA ENLDFERAVE IRNEIKRLTA P
