MODC_MANSM
ID MODC_MANSM Reviewed; 352 AA.
AC Q65SW3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, 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=MS1340;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU37947.1; -; Genomic_DNA.
DR AlphaFoldDB; Q65SW3; -.
DR SMR; Q65SW3; -.
DR STRING; 221988.MS1340; -.
DR EnsemblBacteria; AAU37947; AAU37947; MS1340.
DR KEGG; msu:MS1340; -.
DR eggNOG; COG4148; Bacteria.
DR HOGENOM; CLU_000604_1_1_6; -.
DR OMA; QWLYAQI; -.
DR Proteomes; UP000000607; Chromosome.
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 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 TIGRFAMs; TIGR00638; Mop; 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..352
FT /note="Molybdenum import ATP-binding protein ModC"
FT /id="PRO_0000092543"
FT DOMAIN 2..230
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT DOMAIN 290..352
FT /note="Mop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
SQ SEQUENCE 352 AA; 39307 MW; AEDC65E36CC34C5A CRC64;
MMLEINVKKR LGQLVLNARL TIPGQGITGI FGISGSGKSS LINLVSGLIH PDEGNIRLND
RTLIDTANNI CLAPNQRNIG YVFQDARLFP HYSVKGNLCY GIKRFNQQEF NRIVRLLGIE
HLLARYPLTL SGGEKQRVAI GRALLSNPEM LLMDEPLSAL DLPRKRELLA YLEKLSQEIN
IPILYVTHSL DELFRLADFV VLLDEGKVAA FDSLENLWQS PLFEPWQEQG QKSAVLSLPI
LNHNFSYKMT ALLLGEQQLW VKLLNGDEGK TVRICIRSTD VSITLTVPEK TSIRNILSGK
IITLLPKGNQ VDVKIALGKD EIWASVSTWA AEELQLQIGQ SVYAQIKAVS VM