ID   UVRB_MICLC              Reviewed;         709 AA.
AC   P10125; C5CBM8;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 3.
DT   03-AUG-2022, entry version 140.
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=Mlut_11190;
OS   Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS   NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=465515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2851707; DOI=10.1007/bf00333393;
RA   Shiota S., Nakayama H.;
RT   "Evidence for a Micrococcus luteus gene homologous to uvrB of Escherichia
RT   coli.";
RL   Mol. Gen. Genet. 213:21-29(1988).
RN   [2]
RP   SEQUENCE REVISION.
RA   Nakayama H.;
RL   Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC   2665 / VKM Ac-2230;
RX   PubMed=19948807; DOI=10.1128/jb.01254-09;
RA   Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA   Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA   Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA   Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT   "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT   free-living actinobacterium.";
RL   J. Bacteriol. 192:841-860(2010).
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}.
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DR   EMBL; X12578; CAA31090.1; -; Genomic_DNA.
DR   EMBL; CP001628; ACS30625.1; -; Genomic_DNA.
DR   PIR; S03812; S03812.
DR   RefSeq; WP_010078734.1; NZ_WBMF01000004.1.
DR   AlphaFoldDB; P10125; -.
DR   SMR; P10125; -.
DR   STRING; 465515.Mlut_11190; -.
DR   PRIDE; P10125; -.
DR   EnsemblBacteria; ACS30625; ACS30625; Mlut_11190.
DR   KEGG; mlu:Mlut_11190; -.
DR   PATRIC; fig|465515.4.peg.1061; -.
DR   eggNOG; COG0556; Bacteria.
DR   HOGENOM; CLU_009621_2_1_11; -.
DR   OMA; EYVDRMV; -.
DR   OrthoDB; 95696at2; -.
DR   Proteomes; UP000000738; 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   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; Reference proteome; SOS response.
FT   CHAIN           1..709
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_0000138406"
FT   DOMAIN          35..416
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          438..604
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          666..701
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   MOTIF           101..124
FT                   /note="Beta-hairpin"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   CONFLICT        355
FT                   /note="I -> Y (in Ref. 1; CAA31090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="V -> L (in Ref. 1; CAA31090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="L -> V (in Ref. 1; CAA31090)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   709 AA;  80170 MW;  1FFA79607EBFD4F2 CRC64;
     MSLAQKINRV VAPFEVISPY QPSGDQPKAI AELAERVEAG EKDVVLMGAT GTGKSATTAW
     LVERLQRPTL VMVQNKTLAA QLANEFRELL PNNAVEYFVS YYDYYQPEAY VPQTDTFIEK
     DSSINEEVER LRHSATNALL TRRDVIVVAT VSCIYGLGTP EEYIEQMVTL RRGAEMDRDV
     LLRRFVQMQY VRNDVDFHRG TFRVRGDTVE IIPMYEELAV RIEFFGDEIE SIQTLHPLTG
     QVVREEEEMY IFPASHYVAG DERMGRAITT IEDELRERLQ ELESQDKLLE AQRLRMRTTY
     DLEMMQQMGY CNGIENYSRH IDGRPAGSAP HCLLDYFPDD FLLVVDESHV TIPQIGAMYE
     GDMSRKRTLV EHGFRLPSAM DNRPLKWDEF LERIGQTVYL SATPGAYELG QADGYVEQII
     RPTGLVDPQV VVKPTEGQID DLLEQIRVRT AKDERVLVTT LTKRMAEDLT DYLLEAGVKV
     EYLHSDVDTL RRVELLRELR KGTFDVLVGI NLLREGLDLP EVSLVAILDA DKEGFLRSTT
     SLIQTIGRAA RNVSGEVHMY AGNVTDSMRR AIEETERRRA VQIAYNEEHG IDPQPLRKRI
     ADITDQLARE DADTADFLKG MGGVKSGFDF GMGHRGLSSL DRAPATGEGA AAPAVDPASL
     PAKDLADLIE QMSQQMHQAA ADLQFELAAR LRDEVGELKK ELRQMKREQ