MODC_RHOP2
ID MODC_RHOP2 Reviewed; 377 AA.
AC Q2J1U0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=RPB_0859;
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000250; ABD05570.1; -; Genomic_DNA.
DR RefSeq; WP_011439759.1; NC_007778.1.
DR AlphaFoldDB; Q2J1U0; -.
DR SMR; Q2J1U0; -.
DR STRING; 316058.RPB_0859; -.
DR EnsemblBacteria; ABD05570; ABD05570; RPB_0859.
DR KEGG; rpb:RPB_0859; -.
DR eggNOG; COG4148; Bacteria.
DR HOGENOM; CLU_000604_1_1_5; -.
DR OMA; QWLYAQI; -.
DR OrthoDB; 1200451at2; -.
DR Proteomes; UP000008809; 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 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..377
FT /note="Molybdenum import ATP-binding protein ModC"
FT /id="PRO_0000271686"
FT DOMAIN 4..240
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT DOMAIN 299..369
FT /note="Mop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
SQ SEQUENCE 377 AA; 40103 MW; AD66F4A0A98A50DE CRC64;
MRAIAPRSIR GEFRGRLGGF ALDAAFSVPA TGITGLFGPS GCGKSTVLRC LAGLQRLPGG
RCDVDGDVWQ DEATFLKPHQ RPIGYVFQEA SLFQHLSVRA NLLYGAPRGG ADAAEGAVGF
DEVIELLGLS HLLDRAPRNL SGGERQRVAI GRALLSQPKL LLMDEPLSAL DRLTKDEILP
FLERLHARLS LPVIYVSHDI TEIERLADHL ILMRAGKVLA AGPLTELQSD PALPLATARD
AAVNVDAIAE SYDSVYGLLT LRLDGGRLLV PSAPVQPGEA RRIRIAAGDV SLAREAPHRT
SILNILPARI ATTSPVGPNE VLVVLALGPG GQGARLLARV TRRSWDQLQL AAGDELFAQI
KGVALAPERG AARDSAS