MODC_THIDA
ID MODC_THIDA Reviewed; 362 AA.
AC Q3SJC6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=Tbd_1285;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97238.1; -; Genomic_DNA.
DR RefSeq; WP_011311797.1; NC_007404.1.
DR AlphaFoldDB; Q3SJC6; -.
DR SMR; Q3SJC6; -.
DR STRING; 292415.Tbd_1285; -.
DR PRIDE; Q3SJC6; -.
DR EnsemblBacteria; AAZ97238; AAZ97238; Tbd_1285.
DR KEGG; tbd:Tbd_1285; -.
DR eggNOG; COG4148; Bacteria.
DR HOGENOM; CLU_000604_1_1_4; -.
DR OMA; QWLYAQI; -.
DR OrthoDB; 1200451at2; -.
DR Proteomes; UP000008291; 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; Reference proteome; Translocase; Transport.
FT CHAIN 1..362
FT /note="Molybdenum import ATP-binding protein ModC"
FT /id="PRO_0000271696"
FT DOMAIN 4..238
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 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
SQ SEQUENCE 362 AA; 39244 MW; 5C25F3755E9081EB CRC64;
MSGAGEAAIR ARFRLDWPGF ALDVDLDLPG QGVTALFGHS GSGKTTLLRC IAGLERAAEG
ELRVRGEVWQ DATRFVPTHR RPLGYVFQEA SLFPHLSARG NLEYGMKRSR EPLARAALDD
VVGLLGIGRL LDRRPEQLSG GERQRVAIAR ALAVKPRLLL MDEPLAALDF ARKQEVLPYL
ERLHDELDIP VLYVSHAPDE VARLADHLVV MQDGRAHASG PLGDTLARLD LPIRLGEDVG
VVLDAVVAAR DPAWHLVEMA FAGGRLWARD NGQPLGHRGR VRILARDVSL SRAPVSGTSI
LNTLPAVVVD SVDDGHPALV LVKLRVGDSP LLARLTRRSA HALELAPGRQ VYAQIKAVAL
VG