YPVA_BACSU
ID YPVA_BACSU Reviewed; 641 AA.
AC P50831;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable ATP-dependent helicase YpvA;
DE EC=3.6.4.12;
GN Name=ypvA; OrderedLocusNames=BSU22150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
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).
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 -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC {ECO:0000305}.
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DR EMBL; L47838; AAB38475.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14132.1; -; Genomic_DNA.
DR PIR; C69943; C69943.
DR RefSeq; NP_390097.1; NC_000964.3.
DR RefSeq; WP_003230718.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P50831; -.
DR SMR; P50831; -.
DR STRING; 224308.BSU22150; -.
DR PaxDb; P50831; -.
DR PRIDE; P50831; -.
DR EnsemblBacteria; CAB14132; CAB14132; BSU_22150.
DR GeneID; 939060; -.
DR KEGG; bsu:BSU22150; -.
DR PATRIC; fig|224308.179.peg.2419; -.
DR eggNOG; COG1199; Bacteria.
DR InParanoid; P50831; -.
DR OMA; PRRAQNY; -.
DR PhylomeDB; P50831; -.
DR BioCyc; BSUB:BSU22150-MON; -.
DR Proteomes; UP000001570; Chromosome.
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:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..641
FT /note="Probable ATP-dependent helicase YpvA"
FT /id="PRO_0000102008"
FT DOMAIN 29..303
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 257..260
FT /note="DEGH box"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 641 AA; 74300 MW; 3BECD3B9B3621AF0 CRC64;
MTTSRLPFSL TKTKNFYEEL NNWIGDVFYD ILPEKGFDLR DEQVFMAFQL ERAFKEKKVM
FAEAGVGTGK TLVYLLFAIS YARYVGKPAI IACADETLIE QLVKKEGDIS KLAEHLDLKI
DTRLSKSHEQ YLCLKKLEKT MQRSDDDKWL DLYESLPSFV HESQAMQRFY PYGDRKQYAN
LSNEEWSDVS YDSFQDCLTC DMRHRCGLTL SRDYYRKSTD LIICSHDFYM EHVWTEESRK
REGQLPLLPD HSAVVFDEGH LLEFAAQKAL TYRVKQSTLE LFLERLLQND IREEFAELIE
DALLANDEFF YVLSEESKEV AGSHRLEIKN DHRVKKAADE LCRLLDKIGE ALVFESEMYT
IDQYELSVVE EYVEQMAYSL SLYQKDAISW LEKKEAESTF VVMPRTVAEV LGEKVFSKKI
PYIFSSATLS EGGSFDYIAD SLGIHDYLSL TVDSPYDYDE QMSINLYAKT DMDAEQKTAE
TIETIKRYKG RTLVLFPSFE ELNEFKELSA AWELPYPIFF EGDEEISSLV EKFQEEEETV
LCSVHLWEGL DIPGDALKNV TIWSLPFPPH DPVFTAKRNG AKKDPFEEVD LPYMLLRVRQ
GIGRLIRSNQ DSGSIHIYAG GENERIIDEV KKVLPVEPHM M