HELD_BACSU
ID HELD_BACSU Reviewed; 774 AA.
AC O32215;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=DNA helicase IV;
DE EC=3.6.4.12;
GN Name=helD; Synonyms=yvgS; OrderedLocusNames=BSU33450;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION AS HELICASE.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=11544244; DOI=10.1128/jb.183.19.5772-5777.2001;
RA Carrasco B., Fernandez S., Petit M.-A., Alonso J.C.;
RT "Genetic recombination in Bacillus subtilis 168: effect of delta helD on
RT DNA repair and homologous recombination.";
RL J. Bacteriol. 183:5772-5777(2001).
RN [3]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=21710567; DOI=10.1002/pmic.201000790;
RA Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA Hecker M., Becher D., Polard P., Noirot P.;
RT "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL Proteomics 11:2992-3001(2011).
CC -!- FUNCTION: Catalyzes the unwinding of duplex DNA in the 3' to 5'
CC direction; this reaction is dependent on the hydrolysis of ATP.
CC {ECO:0000269|PubMed:11544244}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Interacts with the RNA polymerase core.
CC {ECO:0000269|PubMed:21710567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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; AL009126; CAB15350.1; -; Genomic_DNA.
DR PIR; H70040; H70040.
DR RefSeq; NP_391225.1; NC_000964.3.
DR RefSeq; WP_003244180.1; NZ_JNCM01000033.1.
DR PDB; 6VSX; X-ray; 2.00 A; A=608-774.
DR PDB; 6WVK; EM; 3.36 A; H=1-774.
DR PDB; 6ZCA; EM; 4.20 A; H=1-774.
DR PDB; 6ZFB; EM; 3.90 A; H/h=1-774.
DR PDBsum; 6VSX; -.
DR PDBsum; 6WVK; -.
DR PDBsum; 6ZCA; -.
DR PDBsum; 6ZFB; -.
DR AlphaFoldDB; O32215; -.
DR SMR; O32215; -.
DR STRING; 224308.BSU33450; -.
DR PaxDb; O32215; -.
DR PRIDE; O32215; -.
DR EnsemblBacteria; CAB15350; CAB15350; BSU_33450.
DR GeneID; 936037; -.
DR KEGG; bsu:BSU33450; -.
DR PATRIC; fig|224308.179.peg.3630; -.
DR eggNOG; COG3973; Bacteria.
DR InParanoid; O32215; -.
DR OMA; YMQNIVA; -.
DR PhylomeDB; O32215; -.
DR BioCyc; BSUB:BSU33450-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..774
FT /note="DNA helicase IV"
FT /id="PRO_0000361273"
FT DOMAIN 212..610
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT COILED 3..31
FT /evidence="ECO:0000255"
FT BINDING 34..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT HELIX 6..50
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 58..97
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6WVK"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 160..182
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:6WVK"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 202..221
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:6WVK"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:6WVK"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:6WVK"
FT TURN 327..332
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 372..381
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 388..406
FT /evidence="ECO:0007829|PDB:6WVK"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 448..473
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 480..485
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 500..513
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 521..532
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 553..562
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 567..572
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 586..590
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 599..603
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 611..618
FT /evidence="ECO:0007829|PDB:6VSX"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:6VSX"
FT STRAND 638..644
FT /evidence="ECO:0007829|PDB:6VSX"
FT HELIX 645..661
FT /evidence="ECO:0007829|PDB:6VSX"
FT STRAND 666..673
FT /evidence="ECO:0007829|PDB:6VSX"
FT HELIX 674..684
FT /evidence="ECO:0007829|PDB:6VSX"
FT TURN 685..687
FT /evidence="ECO:0007829|PDB:6VSX"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 702..708
FT /evidence="ECO:0007829|PDB:6VSX"
FT HELIX 709..712
FT /evidence="ECO:0007829|PDB:6VSX"
FT STRAND 717..723
FT /evidence="ECO:0007829|PDB:6VSX"
FT TURN 727..729
FT /evidence="ECO:0007829|PDB:6VSX"
FT HELIX 733..743
FT /evidence="ECO:0007829|PDB:6VSX"
FT STRAND 746..758
FT /evidence="ECO:0007829|PDB:6VSX"
FT HELIX 760..763
FT /evidence="ECO:0007829|PDB:6VSX"
FT HELIX 767..769
FT /evidence="ECO:0007829|PDB:6VSX"
FT STRAND 771..773
FT /evidence="ECO:0007829|PDB:6VSX"
SQ SEQUENCE 774 AA; 89926 MW; 3B2491C29E40664F CRC64;
MNQQDKEWKE EQSRIDEVLK ELEKKERFLE TSAGGLKHDI IGLRKSFWED VKVNFDDAHE
AIETMASIKQ QAELLSDREH NHRRMDQQLK RIHQLKKSPY FGRIDFIENG EEQAERIYIG
LASCLDEKEE HFLIYDWRAP ISSLYYNYSP GKAEYEVPGE TIEGEMVLKR QFMIKNGTLK
AMFNTDMTIG DEMLQEVLSH HSDTQMKNIV STIQKEQNQI IRNEKSKILI VQGAAGSGKT
SAALQRVAYL LYRHRGVIDA GQIVLFSPNF LFNSYVSSVL PELGEENMEQ ATFQEYIEHR
LGRKFKCESP FDQLEYCLTE TKGGDFPTRL AGITWKAGLS FQQFINEYVT RLSSEGMIFK
NIIFRGQKLI TKEQIQSYFY SLDQNHSIPN RMEQTAKWLL SELNKLEKKE RRKDWVVHEA
ELLDKEDYLD VYKKLQERKR FSESTFNDYQ REQQLLAAII VKKAFKPLKQ AVRLLAFLDV
TQLYLQLFSG WGGKFQHEKM DAIGELTRSA FTDNKLLYED AAPFLYMQDL IEGRKKNTKI
KHLFIDEAQD YSPFQMAYMR SIFPAASMTV LGDINQSIYA HTINGDQRMD ACFEDEPAEY
VRLKRTYRST RQIVEFTKAM LQDGADIEPF NRSGEMPLVV KTEGHESLCQ KLAQEIGRLK
KKGHETIAVI CKTAHQCIQA HAHMSEYTDV RLIHKENQPF QKGVCVIPVY LAKGIEFDAV
LVYDASEEHY HTEHDRRLLY TACTRAMHML AVFYTGEASP FVTAVPPHLY QIAE
