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   27-MAR-2024, entry version 122.
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; Pseudomonadota; 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   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   OrthoDB; 9775594at2; -.
DR   PhylomeDB; P44206; -.
DR   BioCyc; HINF71421:G1GJ1-1497-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0071281; P:cellular response to iron ion; IBA:GO_Central.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   CDD; cd01142; TroA_e; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR   InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR   PANTHER; PTHR30535:SF37; MOLYBDATE-BINDING PROTEIN MOLA; 1.
DR   PANTHER; PTHR30535; VITAMIN B12-BINDING PROTEIN; 1.
DR   Pfam; PF01497; Peripla_BP_2; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 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
//