MODA_HAEIN
ID MODA_HAEIN Reviewed; 254 AA.
AC P45323;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Molybdate-binding protein ModA {ECO:0000305};
DE AltName: Full=Molybdate/tungstate-binding protein ModA {ECO:0000305};
DE Flags: Precursor;
GN Name=modA; OrderedLocusNames=HI_1693;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-209.
RC STRAIN=A2;
RA McLaughlin R., Abu Kwaik Y., Young R., Spinola S., Apicella M.;
RT "Characterization and sequence of the lsg locus from Haemophilus
RT influenzae.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 25-29.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
CC -!- FUNCTION: Involved in the transport of molybdenum into the cell.
CC {ECO:0000250}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000305}.
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DR EMBL; L42023; AAC23339.1; -; Genomic_DNA.
DR EMBL; M94855; AAA24985.1; -; Genomic_DNA.
DR PIR; A64175; A64175.
DR PIR; S27583; S27583.
DR RefSeq; NP_439835.1; NC_000907.1.
DR RefSeq; WP_005694182.1; NC_000907.1.
DR AlphaFoldDB; P45323; -.
DR SMR; P45323; -.
DR STRING; 71421.HI_1693; -.
DR EnsemblBacteria; AAC23339; AAC23339; HI_1693.
DR KEGG; hin:HI_1693; -.
DR PATRIC; fig|71421.8.peg.1772; -.
DR eggNOG; COG0725; Bacteria.
DR HOGENOM; CLU_065520_3_0_6; -.
DR OMA; VCAPQVP; -.
DR PhylomeDB; P45323; -.
DR BioCyc; HINF71421:G1GJ1-1709-MON; -.
DR PHI-base; PHI:5422; -.
DR Proteomes; UP000000579; 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; ISS:UniProtKB.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR InterPro; IPR005950; ModA.
DR PIRSF; PIRSF004846; ModA; 1.
DR TIGRFAMs; TIGR01256; modA; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; Molybdenum; Periplasm;
KW Reference proteome; Signal; Transport; Tungsten.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:10675023"
FT CHAIN 25..254
FT /note="Molybdate-binding protein ModA"
FT /id="PRO_0000031828"
FT BINDING 33
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT BINDING 61
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT BINDING 146
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT BINDING 173
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT BINDING 191
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT CONFLICT 151
FT /note="E -> A (in Ref. 2; AAA24985)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="K -> Q (in Ref. 2; AAA24985)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="G -> A (in Ref. 2; AAA24985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 27302 MW; 3292D9C1F8274285 CRC64;
MKKLTKISTA LLIAGLGFSF AASAKVTVFA AASMTDALQQ VAKDYAKQNP KNEVVFSFAS
SSTLAKQVEE GAPADIFVSA SNKWMKYLSE KDLTVKETEK VLVGNDLVLI APAKSAVNSV
DIAKGEWINA LKDSYLSVGD PAHVPAGQYA EEALTKLNLW DKVKDRLARG KDVRGALALV
ERAEAPYGIV YSTDAKVSQQ VKTVAVFPAD SHKPVVYPVS IVKGHDNADS RDFLKYLESD
AAKKVLVGYG FSAK
