UVRB_METMA
ID UVRB_METMA Reviewed; 670 AA.
AC Q8PRZ9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=MM_3289;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM32985.1; -; Genomic_DNA.
DR RefSeq; WP_011035178.1; NC_003901.1.
DR AlphaFoldDB; Q8PRZ9; -.
DR SMR; Q8PRZ9; -.
DR STRING; 192952.MM_3289; -.
DR PRIDE; Q8PRZ9; -.
DR EnsemblBacteria; AAM32985; AAM32985; MM_3289.
DR GeneID; 24878107; -.
DR KEGG; mma:MM_3289; -.
DR PATRIC; fig|192952.21.peg.3821; -.
DR eggNOG; arCOG04748; Archaea.
DR HOGENOM; CLU_009621_2_1_2; -.
DR OMA; EYVDRMV; -.
DR Proteomes; UP000000595; 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..670
FT /note="UvrABC system protein B"
FT /id="PRO_0000138455"
FT DOMAIN 51..433
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 453..612
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 631..666
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 117..140
FT /note="Beta-hairpin"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 670 AA; 77691 MW; C53D15B2210746EA CRC64;
MKVSSQTTGE LAENKFETIY DERYWESPPF KLVSDFEPKG SQPEAIEKLV DGLKKGEPFQ
TLLGVTGSGK TYTVANVINQ IRKPTLVIAH NKTLAAQLYN EFREFFPENR VEYFVSYYDY
YQPESYLPAK DQYIEKDAMI NPKIEQMRLA ATASLMSRQD VIVVASVSCI YGLGNPENFQ
KMGFELKVGD KVHRKEILEK LIDIQFERND LELMPGRFRV KGDTIDIIPG YFDDIIRIEL
FGDEVDRISE VDKQTGQRKE DMDYFFVYPA RHYVIPEEEQ KSAIQFILEE LEERLPELGL
LESHRLKQRT LYDMEMIQET GSCKGIENYS RHFDHRQPGE KPFCLLDYFP DDFLLVIDES
HQTIPQLHGM YNGDRSRKKS LVDYGFRLPS AFDNRPLKFE EFEKYMKNVI FVSATPADYE
REHSSRVVEQ IIRPTGLVDP EVEVRPLEGQ VRDVMQEIRK IVERGDRALV TTLTKKLAEE
LTEFLAKNEI KARYLHSDIK TIERTEIIRE LRLGKFDVLV GINLLREGLD IPEVGFIGIL
DADKEGFLRN SKSLIQIIGR AARNSSSRVV LYADNMTDSI KSAVQETERR RSMQIAYNEE
HGIVPTTIRK PIREKVVDIT DTKHIPKTDI PNVIIELDAE MREAADRLDF ERAIQVRELI
KKLEKEIKAV
