YJCD_BACSU
ID YJCD_BACSU Reviewed; 759 AA.
AC O31626;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Putative ATP-dependent DNA helicase YjcD;
DE EC=3.6.4.12;
GN Name=yjcD; OrderedLocusNames=BSU11820;
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 POSSIBLE 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).
CC -!- FUNCTION: May be involved in the generation of recombinogenic
CC substrates for the subsequent action of RecA.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13039.3; -; Genomic_DNA.
DR PIR; D69846; D69846.
DR RefSeq; NP_389064.2; NC_000964.3.
DR RefSeq; WP_003245380.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31626; -.
DR SMR; O31626; -.
DR STRING; 224308.BSU11820; -.
DR PaxDb; O31626; -.
DR PRIDE; O31626; -.
DR EnsemblBacteria; CAB13039; CAB13039; BSU_11820.
DR GeneID; 939813; -.
DR KEGG; bsu:BSU11820; -.
DR PATRIC; fig|224308.179.peg.1273; -.
DR eggNOG; COG0210; Bacteria.
DR InParanoid; O31626; -.
DR OMA; YRHFVVD; -.
DR BioCyc; BSUB:BSU11820-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; 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; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..759
FT /note="Putative ATP-dependent DNA helicase YjcD"
FT /id="PRO_0000361274"
FT DOMAIN 134..413
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 414..676
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT REGION 68..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 759 AA; 86976 MW; 8FEDE8CFFFA1F5CE CRC64;
MKCARLNDRI IHLHTYSREH YQFLFEEGIK GHLFCSHCGK PVLLRLNIAD PPEFIHRQPG
DFPACEEACE PKPSKEGKKE DDQESGVIRL PKGKAIAADP SPAVTEWHRP RSIKPGTPFV
PKTIEPDTSL FPSVGLNTDQ LKAVTETEGP LLVLAGAGSG KTRVLTARAA HMIEHLGIPP
ENMLLVTFTT KAVAEMKERM ANQYGLQPAK VRRIVTGTFH SLFYKILYHS NSAKWNGEHL
LKMEWQREQY IKKALYEEGI DEKESPVDQA LQQIGFWKNT YVPNERIPLK DEWEKQVYRL
YEHYERQKKE HSQFDFDDMA SACYELFIER PDLLEQYQSR FTYILIDEFQ DINPVQYKIM
QMLASPEQNL CCVGDDDQSI YAFRGSNPSF ILDFQKDYPG AKTIYLTANY RSTHPIVSSA
DIVVKKNKNR YAKTLEAARD DIQVPVLFYP YDEEEEATMV VSDIKEKIQN GASPEDFAVL
YRTNSGGRAI YERLHQSSIP YTADRGVQSF YSRRIVRQIL AYLYASQNED DTEAIKHLLP
ALFLKQSALN TLKALSITED CTMIKALAKL PDLKPFQLDK IKKIVPFFAS LRTMKPVEAI
TFAEGKMGFS EYLKKRGNEG NKLEKGSDDL RDIKVVAKKF KTIPDFLAHV DHMRAAEKNR
TDEHGVQLMT IHRSKGLEFK TVYVLGTVDG SIPHDFSLET ARKGDEAALE EERRLLYVAM
TRAKQHLYLS CPANRRGKTA NRSRFLYPLL QKARQPLHH