MOLA_HAEIN
ID MOLA_HAEIN Reviewed; 351 AA.
AC P44206;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Molybdate-binding protein MolA {ECO:0000305};
DE AltName: Full=Molybdate/tungstate-binding protein MolA {ECO:0000305};
DE Flags: Precursor;
GN Name=molA {ECO:0000303|PubMed:22078568}; OrderedLocusNames=HI_1472;
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 IDENTIFICATION BY MASS SPECTROMETRY.
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).
RN [3]
RP SUBUNIT.
RX PubMed=20173761; DOI=10.1038/nsmb.1770;
RA Lewinson O., Lee A.T., Locher K.P., Rees D.C.;
RT "A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the
RT dynamics of complex formation.";
RL Nat. Struct. Mol. Biol. 17:332-338(2010).
RN [4]
RP SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=23513215; DOI=10.1073/pnas.1213598110;
RA Vigonsky E., Ovcharenko E., Lewinson O.;
RT "Two molybdate/tungstate ABC transporters that interact very differently
RT with their substrate binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5440-5445(2013).
RN [5]
RP SUBUNIT, AND DOMAIN.
RX PubMed=23709218; DOI=10.1074/jbc.m113.483495;
RA Rice A.J., Alvarez F.J., Schultz K.M., Klug C.S., Davidson A.L.,
RA Pinkett H.W.;
RT "EPR spectroscopy of MolB2C2-a reveals mechanism of transport for a
RT bacterial type II molybdate importer.";
RL J. Biol. Chem. 288:21228-21235(2013).
RN [6]
RP FUNCTION.
RX PubMed=24722984; DOI=10.1074/jbc.m114.563783;
RA Rice A.J., Harrison A., Alvarez F.J., Davidson A.L., Pinkett H.W.;
RT "Small substrate transport and mechanism of a molybdate ATP binding
RT cassette transporter in a lipid environment.";
RL J. Biol. Chem. 289:15005-15013(2014).
RN [7] {ECO:0007744|PDB:3PSA, ECO:0007744|PDB:3PSH}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 22-347 IN COMPLEX WITH MOLYBDATE
RP AND TUNGSTATE, AND FUNCTION.
RX PubMed=22078568; DOI=10.1016/j.str.2011.10.004;
RA Tirado-Lee L., Lee A., Rees D.C., Pinkett H.W.;
RT "Classification of a Haemophilus influenzae ABC transporter HI1470/71
RT through its cognate molybdate periplasmic binding protein, MolA.";
RL Structure 19:1701-1710(2011).
CC -!- FUNCTION: Part of the ABC transporter complex MolBCA involved in
CC molybdate import (PubMed:22078568, PubMed:24722984). Functions as a
CC low-affinity molybdate transporter (PubMed:24722984). Binds to both
CC molybdate and tungstate, but not to sulfate or phosphate
CC (PubMed:22078568). {ECO:0000269|PubMed:22078568,
CC ECO:0000269|PubMed:24722984}.
CC -!- ACTIVITY REGULATION: The MolBCA complex shows a decrease in affinity in
CC the presence of increasing concentrations of substrate and nucleotide.
CC {ECO:0000269|PubMed:23513215}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MolC),
CC two transmembrane proteins (MolB) and a solute-binding protein (MolA).
CC {ECO:0000269|PubMed:20173761, ECO:0000269|PubMed:23513215,
CC ECO:0000269|PubMed:23709218}.
CC -!- INTERACTION:
CC P44206; Q57130: molB; NbExp=2; IntAct=EBI-15837683, EBI-9013882;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- DOMAIN: Nucleotide binding is coupled to a conformational shift at the
CC periplasmic gate. This shift is akin to unlocking a swinging door:
CC allowing just enough space for molybdate to slip into the cell. The
CC lower cytoplasmic gate, identified as gate I, remains open throughout
CC the MolBC-A mechanism, and cytoplasmic gate II closes in the presence
CC of nucleotide. {ECO:0000269|PubMed:23709218}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC23120.1; -; Genomic_DNA.
DR PIR; I64030; I64030.
DR RefSeq; NP_439623.1; NC_000907.1.
DR RefSeq; WP_005693488.1; NC_000907.1.
DR PDB; 3PSA; X-ray; 1.70 A; A=22-347.
DR PDB; 3PSH; X-ray; 1.50 A; A=22-347.
DR PDBsum; 3PSA; -.
DR PDBsum; 3PSH; -.
DR AlphaFoldDB; P44206; -.
DR SMR; P44206; -.
DR DIP; DIP-58992N; -.
DR IntAct; P44206; 2.
DR STRING; 71421.HI_1472; -.
DR EnsemblBacteria; AAC23120; AAC23120; HI_1472.
DR KEGG; hin:HI_1472; -.
DR PATRIC; fig|71421.8.peg.1539; -.
DR eggNOG; COG0614; Bacteria.
DR HOGENOM; CLU_038034_13_0_6; -.
DR OMA; HAGAYNV; -.
DR PhylomeDB; P44206; -.
DR BioCyc; HINF71421:G1GJ1-1497-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion transport; Molybdenum; Periplasm; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..351
FT /note="Molybdate-binding protein MolA"
FT /id="PRO_0000013972"
FT DOMAIN 41..322
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT BINDING 47..48
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:22078568,
FT ECO:0007744|PDB:3PSH"
FT BINDING 217
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:22078568,
FT ECO:0007744|PDB:3PSH"
FT BINDING 264
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:22078568,
FT ECO:0007744|PDB:3PSH"
FT BINDING 300..301
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:22078568,
FT ECO:0007744|PDB:3PSH"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:3PSH"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 153..172
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:3PSH"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:3PSH"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3PSH"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:3PSH"
FT HELIX 328..339
FT /evidence="ECO:0007829|PDB:3PSH"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:3PSH"
SQ SEQUENCE 351 AA; 39205 MW; 166842B3F4D2BBED CRC64;
MKLKSLLIAC LLSSLSFSAL ADRIITDQLD RKVTIPDHIN RAVVLQHQTL NIAVQLDATK
QIVGVLSNWK KQLGKNYVRL APELENMAMP GDLNSVNIES LLALKPDVVF VTNYAPSEMI
KQISDVNIPV VAISLRTGEV GEKGKLNPTL TDEDKAYNDG LKQGIELIAE VFEKKQQGDE
LVKAAFANRK LLADRLGDVS ADKRVRTYMA NPDLGTYGSG KYTGLMMEHA GAYNVAAATI
KGFKQVSLEN VLEWNPAVIL VQDRYPDVVP QILNDQGWAN IQALKDKKVF LMPEYAKAWG
YPMPEALALG EVWLAKALYP QRFQDVDLDK MVNDYYQKFY RTSYKPDNAA R
