MODA_PSEAE
ID MODA_PSEAE Reviewed; 251 AA.
AC Q9I2N2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Tungstate/molybdate/chromate-binding protein ModA {ECO:0000305};
DE Flags: Precursor;
GN Name=modA {ECO:0000303|PubMed:25172858};
GN OrderedLocusNames=PA1863 {ECO:0000312|EMBL:AAG05252.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=25172858; DOI=10.1128/aem.02465-14;
RA Pederick V.G., Eijkelkamp B.A., Ween M.P., Begg S.L., Paton J.C.,
RA McDevitt C.A.;
RT "Acquisition and role of molybdate in Pseudomonas aeruginosa.";
RL Appl. Environ. Microbiol. 80:6843-6852(2014).
RN [3]
RP FUNCTION AS A BINDING PROTEIN.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=31627455; DOI=10.3390/ijms20205156;
RA Fernandez M., Rico-Jimenez M., Ortega A., Daddaoua A., Garcia Garcia A.I.,
RA Martin-Mora D., Torres N.M., Tajuelo A., Matilla M.A., Krell T.;
RT "Determination of Ligand Profiles for Pseudomonas aeruginosa Solute Binding
RT Proteins.";
RL Int. J. Mol. Sci. 20:5156-5156(2019).
CC -!- FUNCTION: Part of the ABC transporter complex ModABC involved in the
CC transport of molybdenum into the cell (Probable). Binds tungstate and
CC molybdate (PubMed:31627455, PubMed:25172858). Can also bind chromate,
CC with lower affinity (PubMed:31627455). Plays an essential role in
CC recruitment of molybdate for nitrate reduction (PubMed:25172858).
CC {ECO:0000269|PubMed:25172858, ECO:0000269|PubMed:31627455,
CC ECO:0000305|PubMed:25172858}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ModC),
CC two transmembrane proteins (ModB) and a solute-binding protein (ModA).
CC {ECO:0000250|UniProtKB:P37329}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P37329}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene reduces cellular molybdate
CC concentrations and results in inhibition of anaerobic growth and
CC nitrate reduction. {ECO:0000269|PubMed:25172858}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000305}.
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DR EMBL; AE004091; AAG05252.1; -; Genomic_DNA.
DR PIR; B83413; B83413.
DR RefSeq; NP_250554.1; NC_002516.2.
DR RefSeq; WP_003113613.1; NZ_QZGE01000003.1.
DR AlphaFoldDB; Q9I2N2; -.
DR SMR; Q9I2N2; -.
DR STRING; 287.DR97_13; -.
DR PaxDb; Q9I2N2; -.
DR PRIDE; Q9I2N2; -.
DR EnsemblBacteria; AAG05252; AAG05252; PA1863.
DR GeneID; 877661; -.
DR KEGG; pae:PA1863; -.
DR PATRIC; fig|208964.12.peg.1938; -.
DR PseudoCAP; PA1863; -.
DR HOGENOM; CLU_065520_1_0_6; -.
DR InParanoid; Q9I2N2; -.
DR OMA; YGATGQF; -.
DR PhylomeDB; Q9I2N2; -.
DR BioCyc; PAER208964:G1FZ6-1902-MON; -.
DR PHI-base; PHI:5468; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
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 InterPro; IPR044084; AvModA-like_subst-bd.
DR InterPro; IPR005950; ModA.
DR PIRSF; PIRSF004846; ModA; 1.
DR TIGRFAMs; TIGR01256; modA; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Molybdenum; Periplasm; Reference proteome; Signal;
KW Transport; Tungsten.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..251
FT /note="Tungstate/molybdate/chromate-binding protein ModA"
FT /evidence="ECO:0000255"
FT /id="PRO_5004327030"
FT BINDING 60
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT BINDING 168
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
SQ SEQUENCE 251 AA; 26377 MW; E8CCA51F2BC93534 CRC64;
MTTRLPQLLL ALLASAVSLA ASADEVQVAV AANFTAPIQA IAKEFEKDTG HRLVAAYGAT
GQFYTQIKNG APFQVFLSAD DSTPAKLEQE GEVVPGSRFT YAIGTLALWS PKAGYVDAEG
EVLKSGSFRH LSIANPKTAP YGLAATQAMD KLGLAATLGP KLVEGQNISQ AYQFVSSGNA
ELGFVALSQI YKDGKVATGS AWIVPTELHD PIRQDAVILN KGKDNAAAKA LVDYLKGAKA
AALIKSYGYE L
