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Database: UniProt
Entry: W1DKH2_KLEPN
LinkDB: W1DKH2_KLEPN
Original site: W1DKH2_KLEPN 
ID   W1DKH2_KLEPN            Unreviewed;       296 AA.
AC   W1DKH2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Fido domain-containing protein {ECO:0000259|PROSITE:PS51459};
OS   Klebsiella pneumoniae IS43.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL09888.1, ECO:0000313|Proteomes:UP000019183};
RN   [1] {ECO:0000313|EMBL:CDL09888.1, ECO:0000313|Proteomes:UP000019183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IS43 {ECO:0000313|EMBL:CDL09888.1,
RC   ECO:0000313|Proteomes:UP000019183};
RA   Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT   "Antibiotic resistance diversity of beta-lactamase producers in the General
RT   Hospital Vienna.";
RL   Submitted (OCT-2013) 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:CDL09888.1}.
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DR   EMBL; CBWK010000409; CDL09888.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1DKH2; -.
DR   SMR; W1DKH2; -.
DR   eggNOG; COG2378; Bacteria.
DR   eggNOG; COG3177; Bacteria.
DR   Proteomes; UP000019183; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3290.10; Fido-like domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR003812; Fido.
DR   InterPro; IPR036597; Fido-like_dom_sf.
DR   InterPro; IPR040198; Fido_containing.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13504; FIDO DOMAIN-CONTAINING PROTEIN DDB_G0283145; 1.
DR   PANTHER; PTHR13504:SF38; PROTEIN ADENYLYLTRANSFERASE AQ_AA38-RELATED; 1.
DR   Pfam; PF02661; Fic; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   SUPFAM; SSF140931; Fic-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51459; FIDO; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR640198-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR640198-2}.
FT   DOMAIN          62..204
FT                   /note="Fido"
FT                   /evidence="ECO:0000259|PROSITE:PS51459"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-1"
FT   BINDING         145..152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT   BINDING         182..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT   SITE            18
FT                   /note="Important for autoinhibition of adenylyltransferase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-3"
SQ   SEQUENCE   296 AA;  33301 MW;  C190C23131991AAE CRC64;
     MLRKENRIRT IQASLAIEHN SLSMEQVTAL LEGKRVLAPA KDIQEVRNAI RAYELMPGWH
     AANISDLLTA HKTLMTGLVD RPGALRGGNV GIYRGTQVIH MAPPAAQVPR LIADLLSWLE
     HTELHPLIAS SVFHYEFEFI HPFADGNGRM GRLWQTLILS QWRQELAWLP VETLIHHQQE
     RYYDILGACD KTSDCTLFVT WMLQNILAAL KEGLETSFIV SEEMSEEMSE EIDVKLAPPE
     NAILRLLTEK PELTARALAE ILGISARTVE RHLQGLQAKG RLIRIGAKKG GSWLVK
//
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