MOLC_HAEIN
ID MOLC_HAEIN Reviewed; 253 AA.
AC Q57399; O05064;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Molybdate import ATP-binding protein MolC {ECO:0000305};
DE EC=7.3.2.5 {ECO:0000305|PubMed:24722984};
GN Name=molC {ECO:0000303|PubMed:22078568}; OrderedLocusNames=HI_1470;
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 CATALYTIC ACTIVITY.
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 MOLB, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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 energy coupling to the transport system (PubMed:24722984). Functions as
CC a low-affinity molybdate transporter (PubMed:24722984).
CC {ECO:0000269|PubMed:22078568, ECO:0000269|PubMed:24722984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) +
CC phosphate; Xref=Rhea:RHEA:22020, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36264,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.5;
CC Evidence={ECO:0000305|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 Q57399; Q57130: molB; NbExp=2; IntAct=EBI-9013875, EBI-9013882;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:17158291}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17158291}.
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 ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; L42023; AAC23118.1; -; Genomic_DNA.
DR PIR; F64125; F64125.
DR RefSeq; NP_439621.1; NC_000907.1.
DR RefSeq; WP_005693486.1; NC_000907.1.
DR PDB; 2NQ2; X-ray; 2.40 A; C/D=1-253.
DR PDBsum; 2NQ2; -.
DR AlphaFoldDB; Q57399; -.
DR SMR; Q57399; -.
DR DIP; DIP-58990N; -.
DR IntAct; Q57399; 2.
DR STRING; 71421.HI_1470; -.
DR TCDB; 3.A.1.14.11; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAC23118; AAC23118; HI_1470.
DR KEGG; hin:HI_1470; -.
DR PATRIC; fig|71421.8.peg.1537; -.
DR eggNOG; COG1120; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; THQPNHA; -.
DR PhylomeDB; Q57399; -.
DR BioCyc; HINF71421:G1GJ1-1495-MON; -.
DR BRENDA; 7.3.2.5; 2529.
DR EvolutionaryTrace; Q57399; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR GO; GO:0015412; F:ABC-type molybdate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
KW Ion transport; Membrane; Molybdenum; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..253
FT /note="Molybdate import ATP-binding protein MolC"
FT /id="PRO_0000093207"
FT DOMAIN 5..229
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:2NQ2"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 19..29
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:2NQ2"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:2NQ2"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2NQ2"
SQ SEQUENCE 253 AA; 28520 MW; AC54279C650C39F1 CRC64;
MNKALSVENL GFYYQAENFL FQQLNFDLNK GDILAVLGQN GCGKSTLLDL LLGIHRPIQG
KIEVYQSIGF VPQFFSSPFA YSVLDIVLMG RSTHINTFAK PKSHDYQVAM QALDYLNLTH
LAKREFTSLS GGQRQLILIA RAIASECKLI LLDEPTSALD LANQDIVLSL LIDLAQSQNM
TVVFTTHQPN QVVAIANKTL LLNKQNFKFG ETRNILTSEN LTALFHLPMF EQQAQYKESF
FTHFVPLYKT LLK
