ID A0A1V0GRU3_9RHOB Unreviewed; 252 AA.
AC A0A1V0GRU3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 2.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:ARC36553.2};
GN Name=modA {ECO:0000313|EMBL:ARC36553.2};
GN ORFNames=A6J80_09315 {ECO:0000313|EMBL:ARC36553.2};
OS Paracoccus yeei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC36553.2, ECO:0000313|Proteomes:UP000191257};
RN [1] {ECO:0000313|Proteomes:UP000191257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA Geyer C., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-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; CP020442; ARC36553.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0GRU3; -.
DR STRING; 147645.A6J80_09315; -.
DR KEGG; pye:A6J80_09315; -.
DR eggNOG; COG0725; Bacteria.
DR Proteomes; UP000191257; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR005950; ModA.
DR NCBIfam; TIGR01256; modA; 1.
DR PANTHER; PTHR30632; MOLYBDATE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR30632:SF17; MOLYBDATE-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:UP000191257};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..252
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015183762"
FT BINDING 35
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 62
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 143
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 170
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 188
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 252 AA; 26097 MW; 3DC4B79B01F14CCE CRC64;
MEPTMRLFQP LIAAALVALA PAAQADEITV FAAASLKDAL DQIAADWQKS HADTVVISYA
GSSKLAKQIQ EGAPADLFIS ASSQWMDAVE TSGDIDAATR LDLLGNTLVL VGTGQPAAAP
VEDLPTLLGK RKLAMAMVDS VPAGQYGKQA LTTLGLWDKV QGQVAQADDV RAALKLVATG
EVPLGIVYGS DAVAEKGVGV VATFPADSHA PITYPAAVTK AADTPQAKLF LDSLKQDPAR
SIFQAQGFTV AE
//
