ID A0A2N7QM93_9GAMM Unreviewed; 259 AA.
AC A0A2N7QM93;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Molybdate-binding periplasmic protein {ECO:0000313|EMBL:PMQ02733.1};
DE Flags: Precursor;
GN Name=modA {ECO:0000313|EMBL:PMQ02733.1};
GN ORFNames=DyAD56_22925 {ECO:0000313|EMBL:PMQ02733.1};
OS Dyella sp. AD56.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1528744 {ECO:0000313|EMBL:PMQ02733.1, ECO:0000313|Proteomes:UP000235676};
RN [1] {ECO:0000313|EMBL:PMQ02733.1, ECO:0000313|Proteomes:UP000235676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD56 {ECO:0000313|EMBL:PMQ02733.1,
RC ECO:0000313|Proteomes:UP000235676};
RA Schulz-Bohm K., Janssens T.K., De Jager V., Gawehns F., De Boer W.,
RA Garbeva P.;
RT "Bacterial performance in fungal presence.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000256|ARBA:ARBA00009175}.
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:PMQ02733.1}.
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DR EMBL; NRDP01000039; PMQ02733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7QM93; -.
DR Proteomes; UP000235676; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030973; F:molybdate ion binding; IEA:InterPro.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR CDD; cd13539; PBP2_AvModA; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR044084; AvModA-like_subst-bd.
DR InterPro; IPR005950; ModA.
DR NCBIfam; TIGR01256; modA; 1.
DR PANTHER; PTHR30632; MOLYBDATE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR30632:SF14; TUNGSTATE_MOLYBDATE_CHROMATE-BINDING PROTEIN MODA; 1.
DR Pfam; PF13531; SBP_bac_11; 1.
DR PIRSF; PIRSF004846; ModA; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004846-1};
KW Molybdenum {ECO:0000256|PIRSR:PIRSR004846-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000235676};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..259
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014873025"
FT BINDING 65
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 172
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 259 AA; 27580 MW; E53483F18206223C CRC64;
MMMRRLLQGL LAMGAVFASA SMAASADNHI TVAAAADLHQ ALDDVVAAYR HDHPDSRIDV
VYGSSGNLLT QIEQGAPFEI FFSADSNYPQ QLVEHGKAGG TPVPYAFGHL VMWSASIDMR
GVQVADLAQP RFGRIAIANP QHAPYGKRAE QALRAAGVWD KVQSRLVFGD NIAQTAQFAQ
SGNAQVGLVA ESLVINAPVK GTSEPVPASL YEPLKQSFVL TKHGADSPLA RDFASYVQGA
PAKAILSRYG FNLPEDGAH
//