ID C1DGY8_AZOVD Unreviewed; 252 AA.
AC C1DGY8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Periplasmic molybdate-binding protein, ModA2 {ECO:0000313|EMBL:ACO76395.1};
GN Name=modA2 {ECO:0000313|EMBL:ACO76395.1};
GN OrderedLocusNames=Avin_01300 {ECO:0000313|EMBL:ACO76395.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO76395.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO76395.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000256|ARBA:ARBA00009175}.
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DR EMBL; CP001157; ACO76395.1; -; Genomic_DNA.
DR RefSeq; WP_012698823.1; NC_012560.1.
DR AlphaFoldDB; C1DGY8; -.
DR STRING; 322710.Avin_01300; -.
DR EnsemblBacteria; ACO76395; ACO76395; Avin_01300.
DR KEGG; avn:Avin_01300; -.
DR eggNOG; COG0725; Bacteria.
DR HOGENOM; CLU_065520_1_0_6; -.
DR OrthoDB; 9785015at2; -.
DR Proteomes; UP000002424; Chromosome.
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..252
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002908669"
FT BINDING 57
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 167
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 252 AA; 26820 MW; 4611B4BA86238C84 CRC64;
MKRLLACLAI ALALPFTAQA NELKVVTATN FLGTLQQLAG EFEKETGHSI TISSGSSGPV
YAQIVNGAPY DVFFSADQKS PEKLDNEGFA LPGSRFTYAI GKLVLWSAKP GLVDDQGKVL
AGNGWRHIAI SNPEIAPYGL AGTQVLTHLG LLDKLTAEKR IVKANSVGQA HSQTASGAAD
LGFVALAQII QKDGSIPGSH WFPPADYYEP IVQQAVIVKS TREKALAEQF MSWMKGPRAV
AIIKAAGYSL PE
//
