ID A0A0R2L312_9LACO Unreviewed; 612 AA.
AC A0A0R2L312;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Diol dehydratase reactivase subunit alpha {ECO:0000313|EMBL:GEK27858.1};
DE SubName: Full=Propanediol utilization ATPase {ECO:0000313|EMBL:KRN96217.1};
GN ORFNames=IV55_GL001603 {ECO:0000313|EMBL:KRN96217.1}, LSI01_01690
GN {ECO:0000313|EMBL:GEK27858.1};
OS Furfurilactobacillus siliginis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Furfurilactobacillus.
OX NCBI_TaxID=348151 {ECO:0000313|EMBL:KRN96217.1, ECO:0000313|Proteomes:UP000051139};
RN [1] {ECO:0000313|EMBL:KRN96217.1, ECO:0000313|Proteomes:UP000051139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22696 {ECO:0000313|EMBL:KRN96217.1,
RC ECO:0000313|Proteomes:UP000051139};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
RN [2] {ECO:0000313|EMBL:GEK27858.1, ECO:0000313|Proteomes:UP000321429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101315 {ECO:0000313|EMBL:GEK27858.1,
RC ECO:0000313|Proteomes:UP000321429};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Lactobacillus siliginis NBRC 101315.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRN96217.1}.
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DR EMBL; BJUD01000002; GEK27858.1; -; Genomic_DNA.
DR EMBL; JQCB01000005; KRN96217.1; -; Genomic_DNA.
DR RefSeq; WP_057810047.1; NZ_JQCB01000005.1.
DR AlphaFoldDB; A0A0R2L312; -.
DR STRING; 348151.IV55_GL001603; -.
DR PATRIC; fig|348151.3.peg.1650; -.
DR OrthoDB; 4676896at2; -.
DR Proteomes; UP000051139; Unassembled WGS sequence.
DR Proteomes; UP000321429; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.90.470.30; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.50.30.70; Swiveling domain of dehydratase reactivase alpha subunit; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR030994; DDR_dom.
DR InterPro; IPR040916; DDR_swiveling.
DR InterPro; IPR009191; DDRA.
DR InterPro; IPR028975; DDRA_swiveling_dom_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR04491; reactive_PduG; 1.
DR Pfam; PF08841; DDR; 1.
DR Pfam; PF18427; DDR_swiveling; 1.
DR PIRSF; PIRSF011502; DdrA_PduG; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF82317; Swiveling domain of dehydratase reactivase alpha subunit; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR011502-2};
KW Magnesium {ECO:0000256|PIRSR:PIRSR011502-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR011502-1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR011502-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051139}.
FT DOMAIN 94..256
FT /note="DD-reactivating factor swiveling"
FT /evidence="ECO:0000259|Pfam:PF18427"
FT DOMAIN 277..604
FT /note="Diol dehydratase reactivase ATPase-like"
FT /evidence="ECO:0000259|Pfam:PF08841"
FT BINDING 12..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 461..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 559..560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
SQ SEQUENCE 612 AA; 64820 MW; 9E5D66D32F5CF5D9 CRC64;
MAQKVIGVDI GNSSTEVALA DVSADGQVDF INSDITATTG IKGTKRNLVG VRTAINGVLA
KSNLDVSDVD LVRINEATPV IGDVAMETIT ETIITESTMI GHNPRTPGGV GLGIGETILI
SDVIRQGNTD TNYVVLVPKE VDFGDAAKLL NAYAANGYKI TGAILQGDDG VLIDNRLNYK
IPIVDEVSLL EKVPQHMLSA IEVADKGGVI RQLSNPYGIA TVFNLTPEQT KNVVPVARAL
IGNRSAVVIK TPAGDVKARV IPAGSINILG DDHQENVGIS DGADKIMKTV SSFKQIDNVT
GESGTNIGGM LERVRQTMAD LTDKKMQDIF IQDLLAVDTS VPNDVKGGLA GEFSMEQAVG
IASMVRTDHL QMQMIADEIQ KEFDVKVEVG GAEAEAAIRG ALTTPGTQAP LAILDLGAGS
SDASIINKEG KIVAIHLAGA GDMTTMIINS ELGLDDVYLA EDIKRYPLAK VESLFYIRHE
DGTVQFFDDA LPGNLFARTV VVKPDGFVPV PGDVSIEKIR SVRQSAKQRV FVTNALRALA
KVSPTGNIRD IPFVVIVGGS ALDFEVPQLV TDALSHYNLV AGRGNVRAIE GPRNAVATGL
ILAYANELKE GR
//