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Database: UniProt
Entry: P37732
LinkDB: P37732
Original site: P37732 
ID   MODC1_AZOVI             Reviewed;         361 AA.
AC   P37732;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   13-SEP-2023, entry version 121.
DE   RecName: Full=Molybdenum import ATP-binding protein ModC 1 {ECO:0000255|HAMAP-Rule:MF_01705};
DE            EC=7.3.2.5 {ECO:0000255|HAMAP-Rule:MF_01705};
GN   Name=modC1 {ECO:0000255|HAMAP-Rule:MF_01705}; Synonyms=modC, modD;
OS   Azotobacter vinelandii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DJ35;
RX   PubMed=8384683; DOI=10.1111/j.1365-2958.1993.tb01136.x;
RA   Luque F., Mitchenall L.A., Chapman M., Christine R., Pau R.N.;
RT   "Characterization of genes involved in molybdenum transport in Azotobacter
RT   vinelandii.";
RL   Mol. Microbiol. 7:447-459(1993).
RN   [2]
RP   GENE NAME.
RX   PubMed=7665518; DOI=10.1128/jb.177.18.5294-5302.1995;
RA   Mouncey N.J., Mitchenall L.A., Pau R.N.;
RT   "Mutational analysis of genes of the mod locus involved in molybdenum
RT   transport, homeostasis, and processing in Azotobacter vinelandii.";
RL   J. Bacteriol. 177:5294-5302(1995).
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=CAA48821.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X69077; CAA48821.1; ALT_INIT; Genomic_DNA.
DR   PIR; S31045; S31045.
DR   RefSeq; WP_012703506.1; NZ_FPKM01000015.1.
DR   AlphaFoldDB; P37732; -.
DR   SMR; P37732; -.
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   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR02142; modC_ABC; 1.
DR   PANTHER; PTHR43514; ABC TRANSPORTER I FAMILY MEMBER 10; 1.
DR   PANTHER; PTHR43514:SF10; MOLYBDENUM IMPORT ATP-BINDING PROTEIN MODC 2; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF03459; TOBE; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; MOP-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..361
FT                   /note="Molybdenum import ATP-binding protein ModC 1"
FT                   /id="PRO_0000092528"
FT   DOMAIN          1..237
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT   DOMAIN          296..361
FT                   /note="Mop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
SQ   SEQUENCE   361 AA;  39769 MW;  06E2ADA0C03BE4A9 CRC64;
     MPADGIRARF RVDYAGFALD VDLTLPGHGV TALFGHSGSG KTTLLRCVAG LERAAEARLE
     INGELWQDSA AGVFLPTHRR ALGYVFQEAS LFPHLSVRRN LEYGMKRVDA ASRQVSWERV
     LELLGIGHLL ERLPGRLSGG ERQRVGIARA LLTSPRLLLM DEPLAALDLK RKNEILPYLE
     RLHDELDIPM LFVSHLPDEV ARLADHVVLL DQGRVTAQGS LQDIMARLDL PTAFHEDAGV
     VIESVVAEHD DHYHLTRLAF PGGAVLVARR PEAPGQRLRL RVHARDVSLA NSRIEDSSIT
     NVLPATVREV VEADTPAHVL VRLEAEGTPL IARITRRSCD QLGIAPGRRM WAQIKAVALL
     G
//
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