ID A0A0R2EGJ7_9LACO Unreviewed; 610 AA.
AC A0A0R2EGJ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE SubName: Full=Pdug protein {ECO:0000313|EMBL:KRN15551.1};
GN ORFNames=FD14_GL002894 {ECO:0000313|EMBL:KRN15551.1};
OS Secundilactobacillus similis DSM 23365 = JCM 2765.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN15551.1, ECO:0000313|Proteomes:UP000051442};
RN [1] {ECO:0000313|EMBL:KRN15551.1, ECO:0000313|Proteomes:UP000051442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN15551.1,
RC ECO:0000313|Proteomes:UP000051442};
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 Genome Announc. 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:KRN15551.1}.
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DR EMBL; AYZM01000178; KRN15551.1; -; Genomic_DNA.
DR RefSeq; WP_057152446.1; NZ_AYZM01000178.1.
DR AlphaFoldDB; A0A0R2EGJ7; -.
DR STRING; 1423804.FD14_GL002894; -.
DR PATRIC; fig|1423804.4.peg.3116; -.
DR OrthoDB; 4676896at2; -.
DR Proteomes; UP000051442; 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:UP000051442}.
FT DOMAIN 93..255
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 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 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 610 AA; 64465 MW; 7F17443C728E1F3E CRC64;
MTRVIGVDIG NSSTEVALAD VTDNGEVTFI NSGIAETTGI KGTKQNLIGV RNSINQVLEK
SHMAISDVDL IRINEATPVI GDVAMETITE TVITESTMIG HNPGTPGGIG TGSGYTVELV
KLLQESDKSR PYIVIIPKEV DFEDAAKLIN AYHASGYNVT AAILQSDDGV LINNRLDKKI
PIVDEVGQID KVPLGMLAAV EVAAPGKVIA QLSNPYGIAT LFDLSSEETK NIVPVSRALI
GNRSAVVIKT PKGDVKARVI PAGKILISGQ PGGRGEVNVA AGADAIMKKI NEFDNIADIA
GESGTNVGGM LEKVRQTMAE LTGKQNSEIA IQDLLAVNTS VPVTVRGGLA GEFSMEEAVG
IAAMVKSDHL QMQQIADLIQ GEFHVPVEIG GAEAESAILG ALTTPGTTKP IAILDLGAGS
TDASIINQKD EKVAIHLAGA GDMVTMIINS ELGLEDPYLA EDIKKYPLAK VDNLFQLRHE
DGAVQFFEDP LPAELFARVV AVKPDGYEPL PGNLSIEKVK IVRQTAKKRV FVTNAIRSLH
HVSPTGNIRD IPFVVIVGGS ALDFEIPQLV TDELSHYNLV AGRGNIRAVE GPRNAVATGL
ILSYASEKRG
//
