MODC_ECOLI
ID MODC_ECOLI Reviewed; 352 AA.
AC P09833;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 4.
DT 03-AUG-2022, entry version 186.
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}; Synonyms=chlD, narD;
GN OrderedLocusNames=b0765, JW0748;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7665460; DOI=10.1128/jb.177.17.4851-4856.1995;
RA Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U., Gunsalus R.P.,
RA Shanmugam K.T.;
RT "Genetic analysis of the modABCD (molybdate transport) operon of
RT Escherichia coli.";
RL J. Bacteriol. 177:4851-4856(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=8564363; DOI=10.1016/s0944-5013(11)80016-9;
RA Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R.;
RT "Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia
RT coli and modR, a regulatory gene.";
RL Microbiol. Res. 150:347-361(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3553151; DOI=10.1128/jb.169.5.1911-1916.1987;
RA Johann S., Hinton S.M.;
RT "Cloning and nucleotide sequence of the chlD locus.";
RL J. Bacteriol. 169:1911-1916(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(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; Peripheral membrane protein.
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; U27192; AAB60173.1; -; Genomic_DNA.
DR EMBL; M16182; AAA83840.1; -; Genomic_DNA.
DR EMBL; U07867; AAB06895.1; -; Genomic_DNA.
DR EMBL; L34009; AAB00837.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73852.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35429.1; -; Genomic_DNA.
DR PIR; E64812; BVECHD.
DR RefSeq; NP_415286.1; NC_000913.3.
DR RefSeq; WP_000891692.1; NZ_STEB01000028.1.
DR AlphaFoldDB; P09833; -.
DR SMR; P09833; -.
DR BioGRID; 4261147; 9.
DR BioGRID; 849738; 1.
DR ComplexPortal; CPX-4342; Molybdate ABC transporter complex.
DR IntAct; P09833; 2.
DR STRING; 511145.b0765; -.
DR TCDB; 3.A.1.8.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P09833; -.
DR PaxDb; P09833; -.
DR PRIDE; P09833; -.
DR EnsemblBacteria; AAC73852; AAC73852; b0765.
DR EnsemblBacteria; BAA35429; BAA35429; BAA35429.
DR GeneID; 945362; -.
DR KEGG; ecj:JW0748; -.
DR KEGG; eco:b0765; -.
DR PATRIC; fig|1411691.4.peg.1513; -.
DR EchoBASE; EB0150; -.
DR eggNOG; COG4148; Bacteria.
DR HOGENOM; CLU_000604_1_1_6; -.
DR InParanoid; P09833; -.
DR OMA; QWLYAQI; -.
DR PhylomeDB; P09833; -.
DR BioCyc; EcoCyc:MODC-MON; -.
DR BioCyc; MetaCyc:MODC-MON; -.
DR PRO; PR:P09833; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0015412; F:ABC-type molybdate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0015689; P:molybdate ion transport; IC:ComplexPortal.
DR GO; GO:0070614; P:tungstate ion transport; IC:ComplexPortal.
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; Reference proteome; Translocase; Transport.
FT CHAIN 1..352
FT /note="Molybdenum import ATP-binding protein ModC"
FT /id="PRO_0000092537"
FT DOMAIN 1..229
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT DOMAIN 289..352
FT /note="Mop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT CONFLICT 244..250
FT /note="PHYAMTA -> SALRDDR (in Ref. 2; AAB06895 and 3;
FT AAA83840)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..352
FT /note="AALRIRIQASDVSLVLQPPQQTSIRNVLRAKVVNSYDDNGQVEVELEVGGKT
FT LWARISPWARDELAIKPGLWLYAQIKSVSITA -> LRYYPHSGFRCFSWFYNRRSKPA
FT FVTIAGKSC (in Ref. 3; AAA83840/AAB00837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39102 MW; 15D9CAAE511AF7D8 CRC64;
MLELNFSQTL GNHCLTINET LPANGITAIF GVSGAGKTSL INAISGLTRP QKGRIVLNGR
VLNDAEKGIC LTPEKRRVGY VFQDARLFPH YKVRGNLRYG MSKSMVDQFD KLVALLGIEP
LLDRLPGSLS GGEKQRVAIG RALLTAPELL LLDEPLASLD IPRKRELLPY LQRLTREINI
PMLYVSHSLD EILHLADRVM VLENGQVKAF GALEEVWGSS VMNPWLPKEQ QSSILKVTVL
EHHPHYAMTA LALGDQHLWV NKLDEPLQAA LRIRIQASDV SLVLQPPQQT SIRNVLRAKV
VNSYDDNGQV EVELEVGGKT LWARISPWAR DELAIKPGLW LYAQIKSVSI TA
