UVRB_BACSU
ID UVRB_BACSU Reviewed; 661 AA.
AC P37954; O34455;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 157.
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};
DE AltName: Full=Protein DinA;
GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; Synonyms=dinA, uvr;
GN OrderedLocusNames=BSU35170;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-186.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=1744042; DOI=10.1128/jb.173.24.7856-7866.1991;
RA Boylan S.A., Thomas M.D., Price C.W.;
RT "Genetic method to identify regulons controlled by nonessential elements:
RT isolation of a gene dependent on alternate transcription factor sigma B of
RT Bacillus subtilis.";
RL J. Bacteriol. 173:7856-7866(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
RX PubMed=1847907; DOI=10.1128/jb.173.5.1696-1703.1991;
RA Cheo D.L., Bayles K.W., Yasbin R.E.;
RT "Cloning and characterization of DNA damage-inducible promoter regions from
RT Bacillus subtilis.";
RL J. Bacteriol. 173:1696-1703(1991).
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; AF017113; AAC67270.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15534.1; -; Genomic_DNA.
DR EMBL; M80473; AAA22360.1; -; Genomic_DNA.
DR EMBL; M64048; AAA22389.1; -; Genomic_DNA.
DR PIR; G69729; G69729.
DR RefSeq; NP_391397.1; NC_000964.3.
DR RefSeq; WP_003243787.1; NZ_JNCM01000033.1.
DR PDB; 2D7D; X-ray; 2.10 A; A=1-661, B=622-661.
DR PDB; 2NMV; X-ray; 2.95 A; A=1-661, B=622-659.
DR PDB; 3V4R; X-ray; 3.25 A; A/B=1-661.
DR PDBsum; 2D7D; -.
DR PDBsum; 2NMV; -.
DR PDBsum; 3V4R; -.
DR AlphaFoldDB; P37954; -.
DR SMR; P37954; -.
DR STRING; 224308.BSU35170; -.
DR PaxDb; P37954; -.
DR PRIDE; P37954; -.
DR EnsemblBacteria; CAB15534; CAB15534; BSU_35170.
DR GeneID; 936663; -.
DR KEGG; bsu:BSU35170; -.
DR PATRIC; fig|224308.179.peg.3807; -.
DR eggNOG; COG0556; Bacteria.
DR InParanoid; P37954; -.
DR OMA; EYVDRMV; -.
DR PhylomeDB; P37954; -.
DR BioCyc; BSUB:BSU35170-MON; -.
DR EvolutionaryTrace; P37954; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..661
FT /note="UvrABC system protein B"
FT /id="PRO_0000138381"
FT DOMAIN 26..413
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 430..596
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 625..660
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 92..115
FT /note="Beta-hairpin"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT CONFLICT 178
FT /note="D -> A (in Ref. 3; AAA22360)"
FT /evidence="ECO:0000305"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2D7D"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 208..228
FT /evidence="ECO:0007829|PDB:2D7D"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 253..276
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 280..300
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 340..363
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 379..384
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 398..403
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 430..442
FT /evidence="ECO:0007829|PDB:2D7D"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 455..467
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:2D7D"
FT TURN 520..523
FT /evidence="ECO:0007829|PDB:2D7D"
FT TURN 526..529
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 531..539
FT /evidence="ECO:0007829|PDB:2D7D"
FT TURN 540..543
FT /evidence="ECO:0007829|PDB:2D7D"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 558..581
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 622..640
FT /evidence="ECO:0007829|PDB:2D7D"
FT HELIX 644..653
FT /evidence="ECO:0007829|PDB:2D7D"
SQ SEQUENCE 661 AA; 76327 MW; A3C0A862A87F867C CRC64;
MKDRFELVSK YQPQGDQPKA IEKLVKGIQE GKKHQTLLGA TGTGKTFTVS NLIKEVNKPT
LVIAHNKTLA GQLYSEFKEF FPNNAVEYFV SYYDYYQPEA YVPQTDTFIE KDASINDEID
KLRHSATSAL FERRDVIIIA SVSCIYGLGS PEEYREMVVS LRTEMEIERN ELLRKLVDIQ
YARNDIDFQR GTFRVRGDVV EIFPASRDEH CVRVEFFGDE IERIREVDAL TGEILGDRDH
VAIFPASHFV TRAEKMEKAI QNIEKELEEQ LKVMHENGKL LEAQRLEQRT RYDLEMMREM
GFCSGIENYS RHLTLRPPGS TPYTLLDYFP DDFMIVVDES HVTIPQVRGM FNGDQARKQV
LVDHGFRLPS ALDNRPLRFE EFEKHMHNIV YVSATPGPYE IEHTDEMVEQ IIRPTGLLDP
LIDVRPIEGQ IDDLIGEIQA RIERNERVLV TTLTKKMSED LTDYLKEIGI KVNYLHSEIK
TLERIEIIRD LRLGKYDVLV GINLLREGLD IPEVSLVAIL DADKEGFLRS ERSLIQTIGR
AARNAEGRVI MYADKITKSM EIAINETKRR REQQERFNEE HGITPKTINK EIRDVIRATV
AAEDKAEYKT KAAPKLSKMT KKERQKVVEQ MEHEMKEAAK ALDFERAAEL RDLLLELKAE
G
