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
//