ID   MODC_RHOCA              Reviewed;         363 AA.
AC   Q08381;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 114.
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}; Synonyms=molD;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=8491722; DOI=10.1128/jb.175.10.3031-3042.1993;
RA   Wang G., Angermueller S., Klipp W.;
RT   "Characterization of Rhodobacter capsulatus genes encoding a molybdenum
RT   transport system and putative molybdenum-pterin-binding proteins.";
RL   J. Bacteriol. 175:3031-3042(1993).
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; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Molybdate
CC       importer (TC 3.A.1.8) family. {ECO:0000255|HAMAP-Rule:MF_01705}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L06254; AAA71909.1; -; Unassigned_DNA.
DR   PIR; C36914; C36914.
DR   AlphaFoldDB; Q08381; -.
DR   SMR; Q08381; -.
DR   IntAct; Q08381; 1.
DR   GeneID; 31489515; -.
DR   OMA; QWLYAQI; -.
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..363
FT                   /note="Molybdenum import ATP-binding protein ModC"
FT                   /id="PRO_0000092553"
FT   DOMAIN          1..230
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT   DOMAIN          289..359
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   363 AA;  38546 MW;  43CD25E9FB7DDB9A CRC64;
     MISARFSGRQ GDFTLDAAFD VPGQGVTALF GPSGCGKTTV LRCMAGLTRL PGGHLVVNGV
     TWQEGRQITP PHRRAVGYVF QEASLFTHLS VRENLVYGLR RARGPLRISE AEVTQLLGID
     PLLRRPTATL SGGERQRVAI GRALLSQPEL LLMDEPLSAL DRISRDEILP YLERLHASLQ
     MPVILVSHDL SEVERLADTL VLMEAGRVRA AGPIAAMQAD PNLPLIHRPD LAAVIEGVVI
     ALDPAYGLST LQVPGGRIVV PGNLGPIGAR RRLRVPATDV SLGRHAPTDT TILNALPAVI
     LGAEAAEGYQ ITVRLALGAS GEGASLLARV SRKSFDLLGF QPGEQVVARL KAMALSAPAQ
     TGG