MODA_XANAC
ID MODA_XANAC Reviewed; 258 AA.
AC Q8PHA1;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Molybdate-binding protein ModA {ECO:0000303|PubMed:16879982};
DE AltName: Full=Molybdate/tungstate-binding protein ModA {ECO:0000305};
DE Flags: Precursor;
GN Name=modA {ECO:0000303|PubMed:16879982, ECO:0000312|EMBL:AAM38201.1};
GN OrderedLocusNames=XAC3358 {ECO:0000312|EMBL:AAM38201.1};
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486 {ECO:0000312|EMBL:AAM38201.1};
RN [1] {ECO:0000312|EMBL:AAM38201.1, ECO:0000312|Proteomes:UP000000576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306 {ECO:0000312|EMBL:AAM38201.1,
RC ECO:0000312|Proteomes:UP000000576};
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2]
RP FUNCTION, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=16879982; DOI=10.1016/j.pep.2006.06.014;
RA Balan A., Santacruz C.P., Moutran A., Ferreira R.C., Medrano F.J.,
RA Perez C.A., Ramos C.H., Ferreira L.C.;
RT "The molybdate-binding protein (ModA) of the plant pathogen Xanthomonas
RT axonopodis pv. citri.";
RL Protein Expr. Purif. 50:215-222(2006).
RN [3] {ECO:0007744|PDB:2H5Y}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 25-258 IN COMPLEX WITH MOLYBDATE.
RX PubMed=16511325; DOI=10.1107/s1744309106003812;
RA Santacruz C.P., Balan A., Ferreira L.C., Barbosa J.A.;
RT "Crystallization, data collection and phasing of the molybdate-binding
RT protein of the phytopathogen Xanthomonas axonopodis pv. citri.";
RL Acta Crystallogr. F Struct. Biol. Commun. 62:289-291(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 25-258 IN COMPLEX WITH MOLYBDATE,
RP AND PHYLOGENETIC ANALYSIS.
RX PubMed=18088604; DOI=10.1016/j.bbapap.2007.11.013;
RA Balan A., Santacruz-Perez C., Moutran A., Ferreira L.C., Neshich G.,
RA Goncalves Barbosa J.A.;
RT "Crystallographic structure and substrate-binding interactions of the
RT molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv.
RT citri.";
RL Biochim. Biophys. Acta 1784:393-399(2008).
RN [5] {ECO:0007744|PDB:3GZG}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 26-257 OF MUTANT SER-151 IN
RP COMPLEX WITH MOLYBDATE, AND MUTAGENESIS OF ASP-83 AND LYS-151.
RX PubMed=24035743; DOI=10.1016/j.abb.2013.09.003;
RA Santacruz-Perez C., Pegos V.R., Honorato R.V., Verli H., Lindahl E.,
RA Barbosa J.A., Balan A.;
RT "A specific interdomain interaction preserves the structural and binding
RT properties of the ModA protein from the phytopathogen Xanthomonas citri
RT domain interaction and transport in ModA.";
RL Arch. Biochem. Biophys. 539:20-30(2013).
CC -!- FUNCTION: Part of the ABC transporter complex ModABC involved in the
CC transport of molybdenum into the cell (Probable). Binds molybdate and
CC tungstate with high affinity in vitro (PubMed:16879982).
CC {ECO:0000269|PubMed:16879982, ECO:0000305}.
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 -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000305}.
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DR EMBL; AE008923; AAM38201.1; -; Genomic_DNA.
DR RefSeq; WP_011052220.1; NC_003919.1.
DR PDB; 2H5Y; X-ray; 1.70 A; A/B/C=25-258.
DR PDB; 3GZG; X-ray; 1.55 A; A/B/C=26-257.
DR PDBsum; 2H5Y; -.
DR PDBsum; 3GZG; -.
DR AlphaFoldDB; Q8PHA1; -.
DR SMR; Q8PHA1; -.
DR STRING; 190486.XAC3358; -.
DR EnsemblBacteria; AAM38201; AAM38201; XAC3358.
DR GeneID; 66912407; -.
DR KEGG; xac:XAC3358; -.
DR eggNOG; COG0725; Bacteria.
DR HOGENOM; CLU_065520_3_0_6; -.
DR OMA; VCAPQVP; -.
DR EvolutionaryTrace; Q8PHA1; -.
DR Proteomes; UP000000576; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030973; F:molybdate ion binding; IDA:UniProtKB.
DR GO; GO:1901359; F:tungstate binding; IDA:UniProtKB.
DR GO; GO:0015689; P:molybdate ion transport; IC:UniProtKB.
DR InterPro; IPR005950; ModA.
DR PIRSF; PIRSF004846; ModA; 1.
DR TIGRFAMs; TIGR01256; modA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Molybdenum; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..258
FT /note="Molybdate-binding protein ModA"
FT /evidence="ECO:0000255"
FT /id="PRO_5004313373"
FT BINDING 36
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:16511325,
FT ECO:0000269|PubMed:24035743, ECO:0007744|PDB:2H5Y,
FT ECO:0007744|PDB:3GZG"
FT BINDING 63
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:16511325,
FT ECO:0000269|PubMed:24035743, ECO:0007744|PDB:2H5Y,
FT ECO:0007744|PDB:3GZG"
FT BINDING 149
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:16511325,
FT ECO:0000269|PubMed:24035743, ECO:0007744|PDB:2H5Y,
FT ECO:0007744|PDB:3GZG"
FT BINDING 176
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:16511325,
FT ECO:0000269|PubMed:24035743, ECO:0007744|PDB:2H5Y,
FT ECO:0007744|PDB:3GZG"
FT BINDING 194
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:16511325,
FT ECO:0000269|PubMed:24035743, ECO:0007744|PDB:2H5Y,
FT ECO:0007744|PDB:3GZG"
FT MUTAGEN 83
FT /note="D->A: Abolishes an important salt bridge in the
FT molybdate-binding pocket resulting in loss of molybdate-
FT binding."
FT /evidence="ECO:0000269|PubMed:24035743"
FT MUTAGEN 151
FT /note="K->S: Shortens an important salt bridge in the
FT molybdate-binding pocket, but still has similar binding
FT affinity to molybdate as wild-type protein."
FT /evidence="ECO:0000269|PubMed:24035743"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:3GZG"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:3GZG"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3GZG"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:3GZG"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:3GZG"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:3GZG"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:3GZG"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:3GZG"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:3GZG"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:3GZG"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3GZG"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:3GZG"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:3GZG"
SQ SEQUENCE 258 AA; 27234 MW; B0FFD1CC97030EA4 CRC64;
MRMIGFWQRA LCVLMLTLPV LASAQTAPVT VFAAASLKES MDEAATAYEK ATGTPVRVSY
AASSALARQI EQGAPADVFF SADLEWMDYL QQHGLVLPAQ RHNLLGNTLV LVAPASSKLR
VDPRAPGAIA KALGENGRLA VGQTASVPAG KYAAAALRKL GQWDSVSNRL AESESVRAAL
MLVSRGEAPL GIVYGSDARA DAKVRVVATF PDDSHDAIVY PVAALKNSNN PATAAFVSWL
GSKPAKAIFA RRGFSLKD
