MODA_ECOLI
ID MODA_ECOLI Reviewed; 257 AA.
AC P37329;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Molybdate-binding protein ModA {ECO:0000303|PubMed:28150901, ECO:0000303|PubMed:8576221, ECO:0000303|PubMed:9302996};
DE AltName: Full=Molybdate/tungstate-binding protein ModA {ECO:0000305};
DE Flags: Precursor;
GN Name=modA; OrderedLocusNames=b0763, JW0746;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=7860583; DOI=10.1128/jb.177.4.1023-1029.1995;
RA Rech S., Deppenmeier U., Gunsalus R.P.;
RT "Regulation of the molybdate transport operon, modABCD, of Escherichia coli
RT in response to molybdate availability.";
RL J. Bacteriol. 177:1023-1029(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7665460; DOI=10.1128/jb.177.17.4851-4856.1995;
RA Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U., Gunsalus R.P.,
RA Shanmugam K.T.;
RT "Genetic analysis of the modABCD (molybdate transport) operon of
RT Escherichia coli.";
RL J. Bacteriol. 177:4851-4856(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=8564363; DOI=10.1016/s0944-5013(11)80016-9;
RA Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R.;
RT "Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia
RT coli and modR, a regulatory gene.";
RL Microbiol. Res. 150:347-361(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PROTEIN SEQUENCE OF 25-31, FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=8576221; DOI=10.1074/jbc.271.5.2557;
RA Rech S., Wolin C., Gunsalus R.P.;
RT "Properties of the periplasmic ModA molybdate-binding protein of
RT Escherichia coli.";
RL J. Biol. Chem. 271:2557-2562(1996).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8409926; DOI=10.1099/00221287-139-8-1869;
RA Lopez Corcuera G., Bastidas M., Dubourdieu M.;
RT "Molybdenum uptake in Escherichia coli K12.";
RL J. Gen. Microbiol. 139:1869-1875(1993).
RN [9]
RP INDUCTION.
RX PubMed=8550508; DOI=10.1128/jb.178.3.735-744.1996;
RA Grunden A.M., Ray R.M., Rosentel J.K., Healy F.G., Shanmugam K.T.;
RT "Repression of the Escherichia coli modABCD (molybdate transport) operon by
RT ModE.";
RL J. Bacteriol. 178:735-744(1996).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9545596; DOI=10.1016/s0005-2736(98)00003-0;
RA Imperial J., Hadi M., Amy N.K.;
RT "Molybdate binding by ModA, the periplasmic component of the Escherichia
RT coli mod molybdate transport system.";
RL Biochim. Biophys. Acta 1370:337-346(1998).
RN [11]
RP FUNCTION.
RX PubMed=21784948; DOI=10.1128/jb.05056-11;
RA Bevers L.E., Schwarz G., Hagen W.R.;
RT "A molecular basis for tungstate selectivity in prokaryotic ABC transport
RT systems.";
RL J. Bacteriol. 193:4999-5001(2011).
RN [12] {ECO:0000312|PDB:1AMF, ECO:0000312|PDB:1WOD}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 25-257 IN COMPLEXES WITH
RP MOLYBDATE AND TUNGSTATE.
RX PubMed=9302996; DOI=10.1038/nsb0997-703;
RA Hu Y., Rech S., Gunsalus R.P., Rees D.C.;
RT "Crystal structure of the molybdate binding protein ModA.";
RL Nat. Struct. Biol. 4:703-707(1997).
RN [13] {ECO:0000312|PDB:3AXF, ECO:0000312|PDB:3R26}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-257 AND MUTANT CYS-35/CYS-177
RP IN COMPLEX WITH PERRHENATE, FUNCTION, BIOTECHNOLOGY, AND MUTAGENESIS OF
RP ALA-35; SER-36; SER-63; ASP-175; ARG-177; VAL-199 AND VAL-218.
RX PubMed=21861186; DOI=10.1007/s00775-011-0833-4;
RA Aryal B.P., Brugarolas P., He C.;
RT "Binding of ReO4(-) with an engineered MoO4(2-)-binding protein: towards a
RT new approach in radiopharmaceutical applications.";
RL J. Biol. Inorg. Chem. 17:97-106(2012).
RN [14] {ECO:0000312|PDB:4XXU}
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH CHROMATE, FUNCTION,
RP BIOTECHNOLOGY, AND MUTAGENESIS OF SER-36 AND SER-63.
RX PubMed=28150901; DOI=10.1002/cbic.201700051;
RA Karpus J., Bosscher M., Ajiboye I., Zhang L., He C.;
RT "Chromate binding and removal by the molybdate-binding protein ModA.";
RL ChemBioChem 18:633-637(2017).
CC -!- FUNCTION: Part of the ABC transporter complex ModABC involved in the
CC transport of molybdenum into the cell (PubMed:8576221). Binds molybdate
CC with high affinity in vitro and with a similar affinity in vivo
CC (PubMed:21861186, PubMed:28150901, PubMed:9545596, PubMed:8576221,
CC PubMed:21784948, PubMed:8409926). Binds tungstate with high affinity in
CC vitro (PubMed:28150901, PubMed:9545596, PubMed:8576221,
CC PubMed:21784948). Binds unnatural anion perrhenate with high affinity
CC in vitro (PubMed:21861186). Does not bind sulfate, phosphate, arsenate,
CC selenate, chlorate, metavanadate, nitrate, perchlorate, permanganate or
CC carbonate (PubMed:9545596, PubMed:28150901, PubMed:8576221).
CC {ECO:0000269|PubMed:21784948, ECO:0000269|PubMed:21861186,
CC ECO:0000269|PubMed:28150901, ECO:0000269|PubMed:8409926,
CC ECO:0000269|PubMed:8576221, ECO:0000269|PubMed:9545596}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8409926,
CC ECO:0000269|PubMed:8576221, ECO:0000269|PubMed:9545596}.
CC -!- INDUCTION: Expression is up-regulated by molybdate limitation
CC (PubMed:7860583). Repressed by molybdate-bound ModE (PubMed:8550508).
CC {ECO:0000269|PubMed:7860583, ECO:0000269|PubMed:8550508}.
CC -!- DISRUPTION PHENOTYPE: Cells are unable to transport molybdate unless
CC high levels of it is supplied in the culture medium.
CC {ECO:0000269|PubMed:8576221}.
CC -!- BIOTECHNOLOGY: May be useful in radiopharmaceutical applications as an
CC engineered disulfide bond-containing protein with increased affinity
CC for perrhenate (PubMed:21861186). May be used to remove chromate, which
CC is toxic to many biological systems, from environmental aqueous
CC solutions (PubMed:28150901). {ECO:0000303|PubMed:21861186,
CC ECO:0000303|PubMed:28150901}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000305}.
CC -!- CAUTION: According to a report, does not bind chromate
CC (PubMed:8576221). According to another report, binds chromate with high
CC affinity and is able to remove it from an aqueous solution in vitro
CC (PubMed:28150901). {ECO:0000269|PubMed:28150901,
CC ECO:0000269|PubMed:8576221}.
CC -!- CAUTION: The mod operon containing this protein has previously been
CC called the chlD locus. {ECO:0000305}.
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DR EMBL; L34009; AAB00835.1; -; Genomic_DNA.
DR EMBL; U27192; AAB60171.1; -; Genomic_DNA.
DR EMBL; U07867; AAB06893.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73850.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35427.1; -; Genomic_DNA.
DR PIR; C64812; C64812.
DR RefSeq; NP_415284.1; NC_000913.3.
DR RefSeq; WP_000101984.1; NZ_LN832404.1.
DR PDB; 1AMF; X-ray; 1.75 A; A=25-257.
DR PDB; 1WOD; X-ray; 1.75 A; A=25-257.
DR PDB; 3AXF; X-ray; 2.00 A; A/B/C=25-257.
DR PDB; 3R26; X-ray; 1.70 A; A=25-257.
DR PDB; 4XXU; X-ray; 1.43 A; A/B=1-257.
DR PDBsum; 1AMF; -.
DR PDBsum; 1WOD; -.
DR PDBsum; 3AXF; -.
DR PDBsum; 3R26; -.
DR PDBsum; 4XXU; -.
DR AlphaFoldDB; P37329; -.
DR SMR; P37329; -.
DR BioGRID; 4262087; 14.
DR ComplexPortal; CPX-4342; Molybdate ABC transporter complex.
DR IntAct; P37329; 1.
DR STRING; 511145.b0763; -.
DR TCDB; 3.A.1.8.1; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P37329; -.
DR jPOST; P37329; -.
DR PaxDb; P37329; -.
DR PRIDE; P37329; -.
DR EnsemblBacteria; AAC73850; AAC73850; b0763.
DR EnsemblBacteria; BAA35427; BAA35427; BAA35427.
DR GeneID; 945364; -.
DR KEGG; ecj:JW0746; -.
DR KEGG; eco:b0763; -.
DR PATRIC; fig|1411691.4.peg.1515; -.
DR EchoBASE; EB2325; -.
DR eggNOG; COG0725; Bacteria.
DR HOGENOM; CLU_065520_3_0_6; -.
DR InParanoid; P37329; -.
DR OMA; VCAPQVP; -.
DR PhylomeDB; P37329; -.
DR BioCyc; EcoCyc:MODA-MON; -.
DR BioCyc; MetaCyc:MODA-MON; -.
DR EvolutionaryTrace; P37329; -.
DR PRO; PR:P37329; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0015412; F:ABC-type molybdate transporter activity; IC:UniProtKB.
DR GO; GO:0030973; F:molybdate ion binding; IDA:UniProtKB.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:EcoCyc.
DR GO; GO:1901359; F:tungstate binding; IDA:UniProtKB.
DR GO; GO:0015689; P:molybdate ion transport; IMP:EcoCyc.
DR GO; GO:0046687; P:response to chromate; IEA:UniProtKB-KW.
DR GO; GO:0070614; P:tungstate ion transport; IC:ComplexPortal.
DR InterPro; IPR005950; ModA.
DR PIRSF; PIRSF004846; ModA; 1.
DR TIGRFAMs; TIGR01256; modA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromate resistance; Direct protein sequencing;
KW Metal-binding; Molybdenum; Periplasm; Reference proteome; Signal;
KW Transport; Tungsten.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:8576221"
FT CHAIN 25..257
FT /note="Molybdate-binding protein ModA"
FT /id="PRO_0000031827"
FT BINDING 36
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:9302996,
FT ECO:0007744|PDB:1AMF"
FT BINDING 63
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:9302996,
FT ECO:0007744|PDB:1AMF"
FT BINDING 149
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:9302996,
FT ECO:0007744|PDB:1AMF"
FT BINDING 176
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:9302996,
FT ECO:0007744|PDB:1AMF"
FT BINDING 194
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:9302996,
FT ECO:0007744|PDB:1AMF"
FT MUTAGEN 35
FT /note="A->C: About 5-fold increased binding affinity for
FT perrhenate as a result of formation of an intramolecular
FT disulfide bond with mutant C-177, which stabilizes the
FT metal-bound closed conformation, but no increased binding
FT affinity for molybdate; when associated with C-177."
FT /evidence="ECO:0000269|PubMed:21861186"
FT MUTAGEN 36
FT /note="S->A: Loss of chromate removal from a buffered
FT solution; when associated with A-63."
FT /evidence="ECO:0000269|PubMed:28150901"
FT MUTAGEN 36
FT /note="S->C: Loss of binding to perrhenate. Slightly
FT reduced chromate removal from a buffered solution."
FT /evidence="ECO:0000269|PubMed:21861186,
FT ECO:0000269|PubMed:28150901"
FT MUTAGEN 36
FT /note="S->D: Loss of binding to perrhenate. Slightly
FT reduced chromate removal from a buffered solution.
FT Significantly reduced chromate removal from a buffered
FT solution; when associated with D-63."
FT /evidence="ECO:0000269|PubMed:21861186,
FT ECO:0000269|PubMed:28150901"
FT MUTAGEN 36
FT /note="S->E: Slightly reduced chromate removal from a
FT buffered solution."
FT /evidence="ECO:0000269|PubMed:28150901"
FT MUTAGEN 63
FT /note="S->A: Loss of chromate removal from a buffered
FT solution; when associated with A-36."
FT /evidence="ECO:0000269|PubMed:28150901"
FT MUTAGEN 63
FT /note="S->C: Reduced binding affinity for perrhenate."
FT /evidence="ECO:0000269|PubMed:21861186"
FT MUTAGEN 63
FT /note="S->D: Reduced binding affinity for perrhenate.
FT Significantly reduced chromate removal from a buffered
FT solution; when associated with D-36."
FT /evidence="ECO:0000269|PubMed:21861186,
FT ECO:0000269|PubMed:28150901"
FT MUTAGEN 175
FT /note="D->N: Reduced binding affinity for perrhenate."
FT /evidence="ECO:0000269|PubMed:21861186"
FT MUTAGEN 177
FT /note="R->C: About 5-fold increased binding affinity for
FT perrhenate as a result of formation of an intramolecular
FT disulfide bond with mutant C-35, which stabilizes the
FT metal-bound closed conformation, but no increased binding
FT affinity for molybdate; when associated with C-35."
FT /evidence="ECO:0000269|PubMed:21861186"
FT MUTAGEN 199
FT /note="V->A,Y,W: No change in affinity for perrhenate."
FT /evidence="ECO:0000269|PubMed:21861186"
FT MUTAGEN 218
FT /note="V->A,Y,W: No change in affinity for perrhenate."
FT /evidence="ECO:0000269|PubMed:21861186"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:4XXU"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:4XXU"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4XXU"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4XXU"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:4XXU"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:4XXU"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4XXU"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:4XXU"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:4XXU"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4XXU"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:4XXU"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:4XXU"
SQ SEQUENCE 257 AA; 27364 MW; 847DB740EE0564E7 CRC64;
MARKWLNLFA GAALSFAVAG NALADEGKIT VFAAASLTNA MQDIATQFKK EKGVDVVSSF
ASSSTLARQI EAGAPADLFI SADQKWMDYA VDKKAIDTAT RQTLLGNSLV VVAPKASVQK
DFTIDSKTNW TSLLNGGRLA VGDPEHVPAG IYAKEALQKL GAWDTLSPKL APAEDVRGAL
ALVERNEAPL GIVYGSDAVA SKGVKVVATF PEDSHKKVEY PVAVVEGHNN ATVKAFYDYL
KGPQAAEIFK RYGFTIK
