ID   MODC_GRABC              Reviewed;         367 AA.
AC   Q0BQ80;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 97.
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};
GN   OrderedLocusNames=GbCGDNIH1_2124;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI63022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000394; ABI63022.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043454504.1; NC_008343.2.
DR   AlphaFoldDB; Q0BQ80; -.
DR   SMR; Q0BQ80; -.
DR   STRING; 391165.GbCGDNIH1_2124; -.
DR   EnsemblBacteria; ABI63022; ABI63022; GbCGDNIH1_2124.
DR   KEGG; gbe:GbCGDNIH1_2124; -.
DR   eggNOG; COG4148; Bacteria.
DR   HOGENOM; CLU_000604_1_1_5; -.
DR   Proteomes; UP000001963; 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   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   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..367
FT                   /note="Molybdenum import ATP-binding protein ModC"
FT                   /id="PRO_0000271673"
FT   DOMAIN          1..234
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT   DOMAIN          293..366
FT                   /note="Mop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
SQ   SEQUENCE   367 AA;  39013 MW;  11DE54E54984112E CRC64;
     MSSAALEVRL NHRFPGTEID VCFAGRGCTV LFGPSGAGKS TIAMAVAGLM RPDHLHLRVG
     GLDLHDLPPE RRRIGVVFQD ARLFPHLSVL GNLEYGARRA PPGDFPLSGD FPLSREEIMT
     MLGIGALLKR RPATLSGGER QRVAIGRALL SRPHMLVMDE PLASLDQARK QDILPVLRRL
     KAAGLPMLYV THALQEMAYL ADDVVLLETG RVRASGSLGH ISSDPALSGG FGHEAGAVLE
     AVVSGHMPDR GLTILSCAGT EVLVPLQALK PGTGLRVRIP AADVIVATES PGHISLHNIL
     PVVMTDWQPA HLQGKAGTTQ EALVRLALPG GHLLARVTRD AIQRLGLEPG RHVLALIKSV
     AVDVLGP