ID   MODA_RHOCA              Reviewed;         252 AA.
AC   Q08383;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Molybdate-binding protein ModA {ECO:0000305};
DE   AltName: Full=Molybdate/tungstate-binding protein ModA {ECO:0000305};
DE   Flags: Precursor;
GN   Name=modA; Synonyms=molP;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=8491722; DOI=10.1128/jb.175.10.3031-3042.1993;
RA   Wang G., Angermueller S., Klipp W.;
RT   "Characterization of Rhodobacter capsulatus genes encoding a molybdenum
RT   transport system and putative molybdenum-pterin-binding proteins.";
RL   J. Bacteriol. 175:3031-3042(1993).
CC   -!- FUNCTION: Involved in the transport of molybdenum into the cell.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ModC),
CC       two transmembrane proteins (ModB) and a solute-binding protein (ModA).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC       family. {ECO:0000305}.
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DR   EMBL; L06254; AAA71911.1; -; Unassigned_DNA.
DR   PIR; E36914; E36914.
DR   RefSeq; WP_013066306.1; NZ_VIBE01000004.1.
DR   AlphaFoldDB; Q08383; -.
DR   SMR; Q08383; -.
DR   GeneID; 31489513; -.
DR   OMA; DITRPKK; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030973; F:molybdate ion binding; ISS:UniProtKB.
DR   GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR   CDD; cd13539; PBP2_AvModA; 1.
DR   InterPro; IPR044084; AvModA-like_subst-bd.
DR   InterPro; IPR005950; ModA.
DR   PIRSF; PIRSF004846; ModA; 1.
DR   TIGRFAMs; TIGR01256; modA; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Molybdenum; Periplasm; Signal; Transport; Tungsten.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..252
FT                   /note="Molybdate-binding protein ModA"
FT                   /id="PRO_0000031829"
FT   BINDING         64
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:P37329"
FT   BINDING         171
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:P37329"
FT   BINDING         190
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:P37329"
SQ   SEQUENCE   252 AA;  26620 MW;  712E99D874A4D47C CRC64;
     MTQFPQTLRA GATALALVMG LALPAAAGEV IAAVAANFTE PAKEIGALFT EKTGHTVTYA
     FGPSGQFYTQ ITQGAPFEVF LSADASRPKK AVEEGYAVPG SDFTYAVGKL VLWSADPARV
     DDKGAVLKTD LEHVAIADPK SAPYGAAAIE VMQKLGVYET LEPKLVTGKS ISQAYEFAAT
     GNAPVGFVAY SQVIGKEGGS SWMVPQDLYK PIKQDAVLLK TGAEDAAAKA YLDFLKTPEA
     LEIIRKYGYV TE