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Database: UniProt
Entry: A0A0R2L312_9LACO
LinkDB: A0A0R2L312_9LACO
Original site: A0A0R2L312_9LACO 
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
//
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