MOLB_HAEIN
ID MOLB_HAEIN Reviewed; 337 AA.
AC Q57130; O05065;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Molybdate import system permease protein MolB {ECO:0000305};
GN Name=molB {ECO:0000303|PubMed:22078568}; OrderedLocusNames=HI_1471;
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 SUBUNIT, AND DOMAIN.
RX PubMed=19254551; DOI=10.1016/j.bpj.2008.11.035;
RA Weng J., Ma J., Fan K., Wang W.;
RT "Asymmetric conformational flexibility in the ATP-binding cassette
RT transporter HI1470/1.";
RL Biophys. J. 96:1918-1930(2009).
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 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).
RN [5]
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 [6]
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 [7]
RP FUNCTION, AND INDUCTION.
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 [8] {ECO:0007744|PDB:2NQ2}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MOLC, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=17158291; DOI=10.1126/science.1133488;
RA Pinkett H.W., Lee A.T., Lum P., Locher K.P., Rees D.C.;
RT "An inward-facing conformation of a putative metal-chelate-type ABC
RT transporter.";
RL Science 315:373-377(2007).
CC -!- FUNCTION: Part of the ABC transporter complex MolBCA involved in
CC molybdate import (PubMed:22078568, PubMed:24722984). Responsible for
CC the translocation of the substrate across the membrane
CC (PubMed:24722984). Functions as a low-affinity molybdate transporter
CC (PubMed:24722984). {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:17158291, ECO:0000269|PubMed:19254551,
CC ECO:0000269|PubMed:20173761, ECO:0000269|PubMed:23513215,
CC ECO:0000269|PubMed:23709218}.
CC -!- INTERACTION:
CC Q57130; P44206: molA; NbExp=2; IntAct=EBI-9013882, EBI-15837683;
CC Q57130; Q57399: molC; NbExp=2; IntAct=EBI-9013882, EBI-9013875;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:17158291}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17158291}.
CC -!- INDUCTION: Expression is repressed by molybdate.
CC {ECO:0000269|PubMed:24722984}.
CC -!- DOMAIN: The transition from the outward-facing to the inward-facing
CC conformation is realized through the asymmetric motion of individual
CC subunits of the transporter (PubMed:19254551). Nucleotide binding is
CC coupled to a conformational shift at the periplasmic gate. This shift
CC is akin to unlocking a swinging door: allowing just enough space for
CC molybdate to slip into the cell. The lower cytoplasmic gate, identified
CC as gate I, remains open throughout the MolBC-A mechanism, and
CC cytoplasmic gate II closes in the presence of nucleotide
CC (PubMed:23709218). {ECO:0000269|PubMed:19254551,
CC ECO:0000269|PubMed:23709218}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. FecCD subfamily. {ECO:0000305}.
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DR EMBL; L42023; AAC23119.1; -; Genomic_DNA.
DR PIR; G64125; G64125.
DR RefSeq; NP_439622.1; NC_000907.1.
DR RefSeq; WP_005693487.1; NC_000907.1.
DR PDB; 2NQ2; X-ray; 2.40 A; A/B=1-337.
DR PDBsum; 2NQ2; -.
DR AlphaFoldDB; Q57130; -.
DR SMR; Q57130; -.
DR DIP; DIP-58991N; -.
DR IntAct; Q57130; 2.
DR STRING; 71421.HI_1471; -.
DR TCDB; 3.A.1.14.11; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAC23119; AAC23119; HI_1471.
DR KEGG; hin:HI_1471; -.
DR PATRIC; fig|71421.8.peg.1538; -.
DR eggNOG; COG0609; Bacteria.
DR HOGENOM; CLU_013016_0_2_6; -.
DR OMA; SFRMPRI; -.
DR PhylomeDB; Q57130; -.
DR BioCyc; HINF71421:G1GJ1-1496-MON; -.
DR EvolutionaryTrace; Q57130; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IBA:GO_Central.
DR Gene3D; 1.10.3470.10; -; 1.
DR InterPro; IPR037294; ABC_BtuC-like.
DR InterPro; IPR000522; ABC_transptr_permease_BtuC.
DR PANTHER; PTHR30472; PTHR30472; 1.
DR Pfam; PF01032; FecCD; 1.
DR SUPFAM; SSF81345; SSF81345; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Molybdenum; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..337
FT /note="Molybdate import system permease protein MolB"
FT /id="PRO_0000060281"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 26..51
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 52..87
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 88..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 99..113
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 114..116
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 117..140
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 141..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 147..171
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 172..193
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 215..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 235..257
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 258..264
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 265..275
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 276..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 279..304
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 305..310
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TRANSMEM 311..329
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:17158291"
FT TOPO_DOM 330..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17158291"
FT HELIX 7..24
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 62..86
FT /evidence="ECO:0007829|PDB:2NQ2"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 117..139
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 147..170
FT /evidence="ECO:0007829|PDB:2NQ2"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 194..213
FT /evidence="ECO:0007829|PDB:2NQ2"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 235..257
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 279..303
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:2NQ2"
SQ SEQUENCE 337 AA; 36531 MW; 83298CCBCF2DC1F5 CRC64;
MQPDSYPKIL FGLTLLLVIT AVISLGIGRY SLSVPQIGQI LWAKATALEI DPVQQQVIFQ
VRLPRILTAL CVGAGLALSG VVLQGIFRNP LVNPHIIGVT SGSAFGGTLA IFFGFSLYGL
FTSTILFGFG TLALVFLFSF KFNQRSLLML ILIGMILSGL FSALVSLLQY ISDTEEKLPS
IVFWLMGSFA TSNWEKLLFF FVPFLLCSSI LLSLSWRLNL LSLDEKEAKA LGVKMAPLRW
LVIFLSGSLV ACQVAISGSI GWVGLIIPHL SRMLVGANHQ SLLPCTMLVG ATYMLLVDNV
ARSLSDAEIP ISILTALIGA PLFGVLVYKL KRGGMNE
