ID   A0A363RNU4_9BURK        Unreviewed;       251 AA.
AC   A0A363RNU4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:PWB18621.1};
GN   Name=modA {ECO:0000313|EMBL:PWB18621.1};
GN   ORFNames=DCO45_11620 {ECO:0000313|EMBL:PWB18621.1};
OS   Comamonas sp. JNW.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=2170731 {ECO:0000313|EMBL:PWB18621.1, ECO:0000313|Proteomes:UP000251772};
RN   [1] {ECO:0000313|EMBL:PWB18621.1, ECO:0000313|Proteomes:UP000251772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JNW {ECO:0000313|EMBL:PWB18621.1,
RC   ECO:0000313|Proteomes:UP000251772};
RA   Go L.Y., Mitchell J.A.;
RL   Submitted (APR-2018) 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:PWB18621.1}.
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DR   EMBL; QETI01000006; PWB18621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A363RNU4; -.
DR   OrthoDB; 9785015at2; -.
DR   Proteomes; UP000251772; 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:UP000251772};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..251
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016742612"
FT   BINDING         60
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         168
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ   SEQUENCE   251 AA;  26569 MW;  145F29AA84AE9E6D CRC64;
     MIQRRFAPLA LSLLAALAAS AHADEVSVAV AANFTAPMQK IAAEFEKDSG HKAVLSFGAT
     GKFYAQINNG APFGILLAAD DTTPAKLAQE GKGVAASRFT YAIGQLVLWS KQAGYVDDKG
     AVLKMGDYRH IAIANPKLAP YGLAAMETLK NLGLTDQVTP KIVQGENIGQ TYQFAASGNA
     QLGFVALSQV MEDGKLREGS AWMVPSAMHE PIRQDAIVLS SAKDNAAATA LMQYLQGDKA
     RAIIRSYGYG F
//