ID   MODC_HAEI8              Reviewed;         351 AA.
AC   Q4QJQ0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=NTHI1998;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX88747.1; -; Genomic_DNA.
DR   RefSeq; WP_005689729.1; NC_007146.2.
DR   AlphaFoldDB; Q4QJQ0; -.
DR   SMR; Q4QJQ0; -.
DR   EnsemblBacteria; AAX88747; AAX88747; NTHI1998.
DR   KEGG; hit:NTHI1998; -.
DR   HOGENOM; CLU_000604_1_1_6; -.
DR   OMA; QWLYAQI; -.
DR   OrthoDB; 1200451at2; -.
DR   BRENDA; 7.3.2.5; 2529.
DR   Proteomes; UP000002525; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR   GO; GO:0015412; F:ABC-type molybdate transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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   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   TIGRFAMs; TIGR00638; Mop; 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..351
FT                   /note="Molybdenum import ATP-binding protein ModC"
FT                   /id="PRO_0000271674"
FT   DOMAIN          1..229
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT   DOMAIN          289..351
FT                   /note="Mop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
SQ   SEQUENCE   351 AA;  39520 MW;  52751D3A26241282 CRC64;
     MLQINVKKQL GKLALQANIQ VPDQGVTAIF GLSGSGKTSL INLVSGLIQP DEGFIRLNDR
     TLVDMESQES LPTHLRKIGY VFQDARLFPH YTVKGNLRYG MKHVSQDDFN YIVDLLGITH
     LLKRYPLTLS GGEKQRVAIG RALLTDPDIL LMDEPLSALD VPRKRELMQY LERLSKEINI
     PILYVTHSLD ELLRLADRVV LMENGIVQAY DSVEKIWNSP IFAPWKGENE QSSVLALPVH
     LHNPPYKMTA LSLGEQALWI HQVPANVGER VLVCIYSSDV SIILQKPEQT SIRNILRGKI
     TQIEIQDSRV DLAVLVEGNK IWASISKWAQ NELRFAVGQD VYVQIKAVSV M