ID   MODC_BORPA              Reviewed;         369 AA.
AC   Q7W1F4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Molybdenum import ATP-binding protein ModC {ECO:0000255|HAMAP-Rule:MF_01705};
DE            EC=7.3.2.5 {ECO:0000255|HAMAP-Rule:MF_01705};
GN   Name=modC {ECO:0000255|HAMAP-Rule:MF_01705}; OrderedLocusNames=BPP0737;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex ModABC involved in
CC       molybdenum import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01705}.
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:0000255|HAMAP-Rule:MF_01705};
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:0000255|HAMAP-Rule:MF_01705}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01705}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01705}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Molybdate
CC       importer (TC 3.A.1.8) family. {ECO:0000255|HAMAP-Rule:MF_01705}.
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DR   EMBL; BX640425; CAE40146.1; -; Genomic_DNA.
DR   RefSeq; WP_010925958.1; NC_002928.3.
DR   AlphaFoldDB; Q7W1F4; -.
DR   SMR; Q7W1F4; -.
DR   EnsemblBacteria; CAE40146; CAE40146; BPP0737.
DR   GeneID; 56480507; -.
DR   KEGG; bpa:BPP0737; -.
DR   HOGENOM; CLU_000604_1_1_4; -.
DR   OMA; SHSILEM; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0042888; F:molybdenum ion transmembrane transporter activity; IEA:InterPro.
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; IPR015852; ABC_transpr_ModC.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR011868; ModC_ABC_ATP-bd.
DR   InterPro; IPR004606; Mop_domain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005116; Transp-assoc_OB_typ1.
DR   PANTHER; PTHR43514:SF9; PTHR43514:SF9; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF03459; TOBE; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; SSF50331; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02142; modC_ABC; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51241; MODC; 1.
DR   PROSITE; PS51866; MOP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane; Molybdenum;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..369
FT                   /note="Molybdenum import ATP-binding protein ModC"
FT                   /id="PRO_0000092531"
FT   DOMAIN          7..243
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT   DOMAIN          304..369
FT                   /note="Mop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
SQ   SEQUENCE   369 AA;  39988 MW;  14337DBD31C9EFD1 CRC64;
     MPSDFPPGQA GIHARFRVDY PEFSLDVDLR LPGRGVTALF GQSGSGKTTC LRCMAGLAPV
     SDGYLDINGE VWLDSAARRA VPTHKRALGY VFQEASLFEH LDVLANLRYG MKRVPPALRR
     VDLEQATGLL GIGHLLARMP AGLSGGERQR VGIARALLTS PRLLLMDEPL AALDVQRKRE
     ILPYLERLHD ELDIPVIYVS HSPDEVARLA DHLVLLEQGR AVASGPLDAL LTRLDLPMAM
     TDDASVVVTG EAAGFDPGYA LLTLQLPGGR ARLRFVHQAA PAGQRLRVVV HARDVSLALQ
     QPREGSILNV LAVRVLEMAP AANPAHVMVR LDADGTPLLA RITRYSRDRL ALAPGMQAWA
     QIKAVSLLA