ID I3WHT8_BIFBI Unreviewed; 827 AA.
AC I3WHT8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=BBB_0859 {ECO:0000313|EMBL:AFL04451.1};
OS Bifidobacterium bifidum BGN4.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=484020 {ECO:0000313|EMBL:AFL04451.1, ECO:0000313|Proteomes:UP000006173};
RN [1] {ECO:0000313|EMBL:AFL04451.1, ECO:0000313|Proteomes:UP000006173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGN4 {ECO:0000313|EMBL:AFL04451.1,
RC ECO:0000313|Proteomes:UP000006173};
RX PubMed=22887663; DOI=10.1128/JB.00988-12;
RA Yu D.S., Jeong H., Lee D.H., Kwon S.K., Song J.Y., Kim B.K., Park M.S.,
RA Ji G.E., Oh T.K., Kim J.F.;
RT "Complete Genome Sequence of the Probiotic Bacterium Bifidobacterium
RT bifidum Strain BGN4.";
RL J. Bacteriol. 194:4757-4758(2012).
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; CP001361; AFL04451.1; -; Genomic_DNA.
DR AlphaFoldDB; I3WHT8; -.
DR KEGG; bbf:BBB_0859; -.
DR PATRIC; fig|484020.3.peg.848; -.
DR HOGENOM; CLU_023846_0_0_11; -.
DR Proteomes; UP000006173; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.2310.20; RelE-like; 1.
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; IPR035093; RelE/ParE_toxin_dom_sf.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF143011; RelE-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000006173}.
FT DOMAIN 326..615
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT REGION 134..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 347..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 827 AA; 91749 MW; D86EC478CB556056 CRC64;
MNKPVVALGR DLMGSLFDLP KKAQKHATTF LTKFQTNPRS SGINLERIAN AADEKLYSAR
IDQRYRAIIA FQKSSNVYVL LYVGDHDDAY KWAETKKLDV NPNTRAIQLY DMVSQEEIDT
AMREDSQNEV GWGSVAANVP QPNSTVPESV SPPMEDHDGT NHGTTSASAT SAVAAKTPQA
PRQAPEPHTG PLPDTYRALT DNDMRRFGVP DMYVPVMCTR KTWQEFDRWG SMLPKDVFTY
LTLVAEGLSK SEVFGLFDET EGKISDRLGL EQQLPTSSID SGEEADPEDF RAALSSYASQ
QSFVVVQGEA DLKRILDAPL EQWRVFLHPS QRLYVEHDYH GPFRLLGGAG TGKTVVAMHR
AKRLAARLLR NGSHQKVLFT TYSRNLATDI ASNLKLICTA DEFNTIDVVN LDKLVKDLLT
GHGYSGEIWY DGSPDHGTDL DNAWRKAIAS IGVNDPKLTV SFFKSELSQV IVPQQVRNAA
DYMRVLRKGR GTRLNRAQKL AVWQVVETYR RIMQTNNAYD VDTAVQNVVS LLTQGDMPRK
YAHVVVDEGQ DFSTPAYRVI RALVDEGDND IFIVGDAQQR IYGHTAVLSK SGIRIQGRAR
KLRINYRTTE QIRSAADSIF RSSGADVADS VFADVRGIGD ASPATTFDDL DGGESSTGDS
RSLMSGPVPE TRRFASQSDE MDAVREWIYG LCGTAENMAG DEFDGERVDP RNVCVVARSR
YCIDQWREAL NNGLPYGVYR LGRDAENRQR QGIRVATMHR VKGLEFDYVV VVDVNDGVCP
PKPVLQSAGA DSAALNEIYR EERSLIYVAM TRAKKGVLLT GVSAQVG
//
