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Database: UniProt
Entry: A0A3T0I768_9BACI
LinkDB: A0A3T0I768_9BACI
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ID   A0A3T0I768_9BACI        Unreviewed;       266 AA.
AC   A0A3T0I768;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:AZU65180.1};
GN   Name=modA {ECO:0000313|EMBL:AZU65180.1};
GN   ORFNames=CHR53_28045 {ECO:0000313|EMBL:AZU65180.1};
OS   Neobacillus mesonae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1193713 {ECO:0000313|EMBL:AZU65180.1, ECO:0000313|Proteomes:UP000282892};
RN   [1] {ECO:0000313|EMBL:AZU65180.1, ECO:0000313|Proteomes:UP000282892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H20-5 {ECO:0000313|EMBL:AZU65180.1,
RC   ECO:0000313|Proteomes:UP000282892};
RA   Kim S.Y., Song H., Sang M.K., Weon H.-Y., Song J.;
RT   "The complete genome sequence of Bacillus mesonae strain H20-5, an
RT   efficient strain improving plant abiotic stress resistance.";
RL   Submitted (JUL-2017) 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; CP022572; AZU65180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3T0I768; -.
DR   STRING; 1193713.GCA_001636315_02532; -.
DR   KEGG; nmk:CHR53_28045; -.
DR   OrthoDB; 9785015at2; -.
DR   Proteomes; UP000282892; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000282892};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..266
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019579497"
FT   BINDING         48
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         76
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         156
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         183
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         201
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ   SEQUENCE   266 AA;  29440 MW;  080B948831C0F709 CRC64;
     MKRQIVFSIL LLLLIASGCS SESDKQQGQI KHGNKVEKVE LTVSAAASLQ DALNEITTAF
     EKEHQNIKIN YNFGASGALQ QQISQGAPVD LFFSAAEDKF DRLVKNGLIK KENGLNLVGN
     ELVLVVPKEA NKQIQTFEDL PRANRISIGT PESVPAGQYA KDTLENLHIW KDLKDKIVFA
     KDVRQVLTYV ETNNVDAGIV YKTDAMISPK VKIIAAAPEK THAPIIYPVG VIKNSPHQTE
     AMEFYQYLQS PSSIEILEKY GFKGLN
//
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