ID A3CLC8_STRSV Unreviewed; 618 AA.
AC A3CLC8;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 28-JAN-2026, entry version 83.
DE SubName: Full=Propanediol utilization:dioldehydratase reactivation, putative {ECO:0000313|EMBL:ABN43983.1};
GN OrderedLocusNames=SSA_0537 {ECO:0000313|EMBL:ABN43983.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN43983.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN43983.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN43983.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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DR EMBL; CP000387; ABN43983.1; -; Genomic_DNA.
DR RefSeq; WP_011836575.1; NC_009009.1.
DR AlphaFoldDB; A3CLC8; -.
DR STRING; 388919.SSA_0537; -.
DR KEGG; ssa:SSA_0537; -.
DR PATRIC; fig|388919.9.peg.519; -.
DR eggNOG; COG0849; Bacteria.
DR HOGENOM; CLU_449540_0_0_9; -.
DR OrthoDB; 4676896at2; -.
DR Proteomes; UP000002148; Chromosome.
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:UP000002148}.
FT DOMAIN 93..254
FT /note="DD-reactivating factor swiveling"
FT /evidence="ECO:0000259|Pfam:PF18427"
FT DOMAIN 275..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 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 459..462
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 618 AA; 66164 MW; F043FCD85F6EB165 CRC64;
MKRIIGVDIG NSSTESALAE VQDDGSIHFL ASAIADTTGI KGTKENVHGI YQSLRKLMEQ
TSFELGQVDL IRINEATPVI GDVAMETITE TVITESTMIG HNPRTPGGLG LGIGLTVDIL
DLVHHPIDEK YIVVVPKVID FDLVAQLINA YLAKGYQITA AILQADDGVL VNNRISQKIP
IVDEILFIDK VPLGMQAAVE VVEQGKVISQ LSNPYGIATV FGLSAEETKS IVPIARALIG
NRSAVVIKTP AGDVQARTIP AGSIQIIGKE HTLKVDISKG ADEIMEKIVY AGEISNVVGE
AGTNVGGMLE KVRQTMADLT EKEPSDIYIR DLLAVNTFAP ISVRGGVAGE FSMEQAVGIA
SMVNSDKLQM SIIAQEVERE LGITVEIGGA EAEAAILGAL TTPGTDRPLA ILDLGAGSTD
ASIIDSRGQI LAVHLAGAGD MVTMLINSEL GLENHHLAED IKRYPLAKVE SLFHIRHEDG
TVQFFDKPLS GDLFARVVIV KENDEFVPID DGDYSIEKIK LVRQSAKERV FVTNAVRALK
RVSPTQNIRD IPFVVIVGGS ALDFEIPQLV TEALSQHAIV AGRGNVRGLV GPRNAVATGL
ILTYVREKWG ADYGISLY
//
