UVRB_CLAM3
ID UVRB_CLAM3 Reviewed; 688 AA.
AC A5CRU3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=CMM_1750;
OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=443906;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 382;
RX PubMed=18192381; DOI=10.1128/jb.01595-07;
RA Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA Bartels D.;
RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT in pathogenicity.";
RL J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN01806.1; -; Genomic_DNA.
DR RefSeq; WP_012038438.1; NC_009480.1.
DR AlphaFoldDB; A5CRU3; -.
DR SMR; A5CRU3; -.
DR STRING; 443906.CMM_1750; -.
DR EnsemblBacteria; CAN01806; CAN01806; CMM_1750.
DR KEGG; cmi:CMM_1750; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_11; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR Proteomes; UP000001564; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; Helicase; Hydrolase; Nucleotide-binding; SOS response.
FT CHAIN 1..688
FT /note="UvrABC system protein B"
FT /id="PRO_1000077875"
FT DOMAIN 31..188
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 434..587
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 642..677
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT REGION 607..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..120
FT /note="Beta-hairpin"
FT COMPBIAS 607..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 688 AA; 77488 MW; 538F58740601A65E CRC64;
MQPTRSVRPF KVVSDYSPSG DQPTAIAELA GRVNAGEPDV VLLGATGTGK SATAAWLIEK
VQRPTLILAH NKTLAAQLAT EFRELMPDNA VEYFVSYYDY YQPEAYVPQT DTFIEKDSSV
NAEVERLRHS TTNSLLSRRD VVVVSTVSCI YGLGQPEQYM NAMVALQVGM QIDRDTLIRK
FVSMQYQRND VDFSRGNFRV RGDTIEIIPM YEELAIRIEM FGDEIEALYQ LHPLTGDVVR
KMDSVSVFPG SHYVAETEVM RRAIGTIQQE LEERLTVLER EGKLLEAQRL RMRTNFDIEM
MQQIGFCSGI ENYSRHIDGR DAGEAPHCLL DYFPDDFLVV IDESHVTVPQ IGAMFEGDSS
RKRTLVEHGF RLPSALDNRP LKWNEFTERV PQTVYMSATP GKYELGMGDG VVEQIIRPTG
LIDPAIVVKP TKGQIDDLLE QIRIRVEKDE RILVTTLTKK MAEELTDYFA EAGVRVRYLH
SDVDTLRRVE LLSELRAGVY DVLVGINLLR EGLDLPEVSL VAILDADKEG FLRSSTSLIQ
TIGRAARNVS GEVHMYADVL TDSMKRAIEE TDRRREKQVA YNTEHGIDPT PLRKRIADIT
EILAREGEDT KKMLEGRGGG KRSPTPNLRR EGKAAAGANE LETIISDLND QMLQAAGELK
FELAARLRDE LGDLKRELRQ MEKAGHLS
