ID A0A0R1K1U7_9LACO Unreviewed; 613 AA.
AC A0A0R1K1U7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Propanediol utilization ATPase {ECO:0000313|EMBL:KRK77132.1};
GN ORFNames=FD30_GL000493 {ECO:0000313|EMBL:KRK77132.1};
OS Levilactobacillus namurensis DSM 19117.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423773 {ECO:0000313|EMBL:KRK77132.1, ECO:0000313|Proteomes:UP000051162};
RN [1] {ECO:0000313|EMBL:KRK77132.1, ECO:0000313|Proteomes:UP000051162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19117 {ECO:0000313|EMBL:KRK77132.1,
RC ECO:0000313|Proteomes:UP000051162};
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).
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:KRK77132.1}.
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DR EMBL; AZDT01000010; KRK77132.1; -; Genomic_DNA.
DR RefSeq; WP_056943688.1; NZ_AZDT01000010.1.
DR AlphaFoldDB; A0A0R1K1U7; -.
DR STRING; 1423773.FD30_GL000493; -.
DR GeneID; 84781616; -.
DR PATRIC; fig|1423773.3.peg.504; -.
DR OrthoDB; 4676896at2; -.
DR Proteomes; UP000051162; 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}.
FT DOMAIN 93..255
FT /note="DD-reactivating factor swiveling"
FT /evidence="ECO:0000259|Pfam:PF18427"
FT DOMAIN 276..603
FT /note="Diol dehydratase reactivase ATPase-like"
FT /evidence="ECO:0000259|Pfam:PF08841"
FT BINDING 11..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 460..463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 558..559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
SQ SEQUENCE 613 AA; 65426 MW; E13AF60C8D1CEE2E CRC64;
MAKVIGVDIG NSSTEVALAD VSENGEVQFI GSGISATTGI KGTKQNLIGI KKSLRQVLDT
THLELNDIDL IRINEATPVI GDVAMETITE TVITESTMIG HNPNTPGGLG IGSGYTVELL
QLLKQTDKSR KYIVLIPKTI DFEDAAKLIN VYTKAGFQIT AAILQNDDGV LIDNRLESRI
PIVDEVSQID KVPVGMLAAV EVADKGKVIS QLSNPYGIAT LFGLTSDETK NIVPVSRALI
GNRSAVVIKT PEGDVKARVI PAGSIKIEGI RDSDSVNVAA GAEAIMKKIN EFDRIQDITG
ESGTNVGGML EKVRQTMADL TAKQNKDIAI QDLLAVNTSV PVKVQGGLAG EFSTEEAVGI
AAMVKSDHLQ MQVIANLIQD DMHIPVEIGG AEAEAAILGA LTTPGTTKPI AILDLGAGST
DASIINKENQ IVAIHLAGAG DMVTMIINSE LGLDDIYLAE DIKKYPLARV ENLFQIRHED
GTVQFFDKPL PSDIFARTVV IKPDGYVPLP GDLNIEKVKT IRQTAKKRVF VENAQRALKH
VSPTGNIRDI PFVVIVGGSA LDFEIPQLVT DELSHYNLVA GRGNIRSIEG PRNAVATGLI
LSYAQERRGA HVS
//
