ID   MODC_PSESM              Reviewed;         362 AA.
AC   Q881C1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=PSPTO_2975;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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; AE016853; AAO56467.1; -; Genomic_DNA.
DR   RefSeq; NP_792772.1; NC_004578.1.
DR   RefSeq; WP_011104308.1; NC_004578.1.
DR   AlphaFoldDB; Q881C1; -.
DR   SMR; Q881C1; -.
DR   STRING; 223283.PSPTO_2975; -.
DR   EnsemblBacteria; AAO56467; AAO56467; PSPTO_2975.
DR   GeneID; 1184629; -.
DR   KEGG; pst:PSPTO_2975; -.
DR   PATRIC; fig|223283.9.peg.3035; -.
DR   eggNOG; COG4148; Bacteria.
DR   HOGENOM; CLU_000604_1_1_6; -.
DR   OMA; QWLYAQI; -.
DR   OrthoDB; 1200451at2; -.
DR   PhylomeDB; Q881C1; -.
DR   Proteomes; UP000002515; 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; ISS:JCVI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042888; F:molybdenum ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015689; P:molybdate ion transport; ISS:JCVI.
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; Reference proteome; Translocase; Transport.
FT   CHAIN           1..362
FT                   /note="Molybdenum import ATP-binding protein ModC"
FT                   /id="PRO_0000092550"
FT   DOMAIN          2..236
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT   DOMAIN          297..362
FT                   /note="Mop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
SQ   SEQUENCE   362 AA;  39908 MW;  A06B93EA2F8C5EE2 CRC64;
     MVSPIEVRLQ MTYPEFTVST DLALPGAGIT ALFGPSGSGK TTCLRCIAGL EKAEQGFIRV
     HDEVWQDSEN GVFLAPHKRA IGYVFQEASL FDHLSVRANL EFGLKRIPRP QRRIELQQAT
     ELLGIDHLLE RRPDKLSGGE RQRVGIARAL LTSPRLMLLD EPLAALDTKR KGEILPYLER
     LHRELDIPML YVSHAQDEVA RLADHLVLLE AGKVLASGPI RETLARLDLP LAMGDDAGVV
     IEGTVSAYDR HYQLLTVTLP GSNLCMRVAH AELQIGTLLR VKVQARDVSL NLQSDDHSSI
     LNRLPVTVLE EALADNLAHV LVKLNAGGTP LLARITRYSS DQLNLHRGQT LWAQIKAVAV
     LA