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Database: UniProt
Entry: A0A2S0UG99_9BACL
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ID   A0A2S0UG99_9BACL        Unreviewed;       263 AA.
AC   A0A2S0UG99;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:AWB46848.1};
GN   Name=modA {ECO:0000313|EMBL:AWB46848.1};
GN   ORFNames=DCC85_06815 {ECO:0000313|EMBL:AWB46848.1};
OS   Paenibacillus sp. CAA11.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1532905 {ECO:0000313|EMBL:AWB46848.1, ECO:0000313|Proteomes:UP000244407};
RN   [1] {ECO:0000313|EMBL:AWB46848.1, ECO:0000313|Proteomes:UP000244407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAA11 {ECO:0000313|EMBL:AWB46848.1,
RC   ECO:0000313|Proteomes:UP000244407};
RA   Um Y., Kim S., Gong G.;
RT   "Complete genome of CAA11.";
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}.
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DR   EMBL; CP028922; AWB46848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0UG99; -.
DR   OrthoDB; 9785015at2; -.
DR   Proteomes; UP000244407; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR   CDD; cd13537; PBP2_YvgL_like; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR005950; ModA.
DR   InterPro; IPR041879; YvgL-like_PBP2.
DR   NCBIfam; TIGR01256; modA; 1.
DR   PANTHER; PTHR30632; MOLYBDATE-BINDING PERIPLASMIC PROTEIN; 1.
DR   PANTHER; PTHR30632:SF0; SULFATE-BINDING PROTEIN; 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:UP000244407};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   REGION          12..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         71
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         153
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         180
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         198
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ   SEQUENCE   263 AA;  28251 MW;  8E7DC0A540C56479 CRC64;
     MLMLLLAGCG KDSANKESAS NETNKPSAPA TSQVELTISA AASLKDSMEQ LSETYEKSHT
     DVHLVFNYGA SGSLQKQIEQ GAPADIFISA GNKQMQALVD QGLIEAKDSS VLLRNELVLI
     VPKSSSQTPA TLDDLKGEST KLIAMGDPDA VPAGNYTKES LESNKLWDTL KPKMVFAKDV
     RQVLTYVETG NADAGFVYKS DAMISDKVKT AFVVDASAHK PIEYPIGLLK ASKEQEAAQS
     FIKFLESAEA LEVFTKFGFS TVS
//
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