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Database: UniProt
Entry: A0A1V3PZL7_9GAMM
LinkDB: A0A1V3PZL7_9GAMM
Original site: A0A1V3PZL7_9GAMM 
ID   A0A1V3PZL7_9GAMM        Unreviewed;       263 AA.
AC   A0A1V3PZL7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:OOG56533.1};
GN   ORFNames=B0E48_10390 {ECO:0000313|EMBL:OOG56533.1};
OS   Rhodanobacter sp. C03.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1945858 {ECO:0000313|EMBL:OOG56533.1, ECO:0000313|Proteomes:UP000189128};
RN   [1] {ECO:0000313|EMBL:OOG56533.1, ECO:0000313|Proteomes:UP000189128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C03 {ECO:0000313|EMBL:OOG56533.1,
RC   ECO:0000313|Proteomes:UP000189128};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-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:OOG56533.1}.
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DR   EMBL; MUNT01000006; OOG56533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3PZL7; -.
DR   STRING; 1945858.B0E48_10390; -.
DR   OrthoDB; 9785015at2; -.
DR   Proteomes; UP000189128; 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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..263
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012030728"
FT   BINDING         66
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         173
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ   SEQUENCE   263 AA;  27929 MW;  D91FF1BACA1A0E13 CRC64;
     MIKMRALLGG LLALALTLSM HTAHASQPRH MTIAAAADLH YALDAVIAAY HQAHPQDAIE
     VSYGSSGKLL AQIEQGAPFE LFFSADSEYP KQLVAAGAAS GDPVPYALGH IVIWSASVDA
     SKLTVADLAK PSFDHIAIAN PEHAPYGKRA EQALRAAGVW DAVQSRLVYG DNIAQTAQFI
     ASGNAKVGII AQSLALDPQM AKKGSYALIP ATLYQPLLQS FVVTRRGADN TLAHDFARYM
     QGAEARSVLS RYGFSLPSPA VEH
//
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