ID C7NCG9_LEPBD Unreviewed; 218 AA.
AC C7NCG9;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Transcriptional regulator, ArsR family {ECO:0000313|EMBL:ACV39815.1};
GN OrderedLocusNames=Lebu_1953 {ECO:0000313|EMBL:ACV39815.1};
OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS 10249 / C-1013-b).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV39815.1, ECO:0000313|Proteomes:UP000001910};
RN [1] {ECO:0000313|EMBL:ACV39815.1, ECO:0000313|Proteomes:UP000001910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b
RC {ECO:0000313|Proteomes:UP000001910};
RX PubMed=21304648; DOI=10.4056/sigs.1854;
RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT b).";
RL Stand. Genomic Sci. 1:126-132(2009).
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DR EMBL; CP001685; ACV39815.1; -; Genomic_DNA.
DR RefSeq; WP_015770153.1; NC_013192.1.
DR AlphaFoldDB; C7NCG9; -.
DR STRING; 523794.Lebu_1953; -.
DR KEGG; lba:Lebu_1953; -.
DR eggNOG; COG0607; Bacteria.
DR eggNOG; COG0640; Bacteria.
DR HOGENOM; CLU_108527_0_0_0; -.
DR OMA; RIHYRLA; -.
DR OrthoDB; 9800872at2; -.
DR Proteomes; UP000001910; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd00090; HTH_ARSR; 1.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; NF033788; HTH_metalloreg; 1.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 1.
DR Pfam; PF01022; HTH_5; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00778; HTHARSR.
DR SMART; SM00418; HTH_ARSR; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50987; HTH_ARSR_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
FT DOMAIN 8..102
FT /note="HTH arsR-type"
FT /evidence="ECO:0000259|PROSITE:PS50987"
FT DOMAIN 132..214
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 218 AA; 24962 MW; 66B6F223A6FBA9C9 CRC64;
MDKICQNYKN SLYSGLSKIG KCLSSEKRIE ILDLLVQGAK TVESISNETG MSIANTSRHL
QILKDGNLVI SEKKGNYVVY EIANTQIIDL VYLLIGVGEQ QLADIQRIHN EFNDSCMKIR
PITLEQAYEM VKNKETLIID LRPEDEFNSS HIENAINIPM KNLEENLKKL PKNKEIIVYC
RGRNCAYANL ASKFLNDNGF HAYSLNQSYY DWQKYGNI
//