(data stored in ACNUC7421 zone)

SWISSPROT: B7ULN8_ECO27

ID   B7ULN8_ECO27            Unreviewed;       352 AA.
AC   B7ULN8;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   RecName: Full=Molybdenum import ATP-binding protein ModC {ECO:0000256|HAMAP-Rule:MF_01705};
DE            EC=7.3.2.5 {ECO:0000256|HAMAP-Rule:MF_01705};
GN   Name=modC {ECO:0000256|HAMAP-Rule:MF_01705,
GN   ECO:0000313|EMBL:CAS08190.1};
GN   OrderedLocusNames=E2348C_0642 {ECO:0000313|EMBL:CAS08190.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08190.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08190.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Part of the ABC transporter complex ModABC involved in
CC       molybdenum import. Responsible for energy coupling to the
CC       transport system. {ECO:0000256|HAMAP-Rule:MF_01705,
CC       ECO:0000256|SAAS:SAAS00359003}.
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:0000256|HAMAP-Rule:MF_01705,
CC         ECO:0000256|SAAS:SAAS01131827};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins
CC       (ModC), two transmembrane proteins (ModB) and a solute-binding
CC       protein (ModA). {ECO:0000256|HAMAP-Rule:MF_01705,
CC       ECO:0000256|SAAS:SAAS00359027}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01705, ECO:0000256|SAAS:SAAS00055238}; Peripheral membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_01705,
CC       ECO:0000256|SAAS:SAAS00055238}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Molybdate
CC       importer (TC 3.A.1.8) family. {ECO:0000256|HAMAP-Rule:MF_01705,
CC       ECO:0000256|SAAS:SAAS00551695}.
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DR   EMBL; FM180568; CAS08190.1; -; Genomic_DNA.
DR   RefSeq; WP_000891664.1; NC_011601.1.
DR   EnsemblBacteria; CAS08190; CAS08190; E2348C_0642.
DR   KEGG; ecg:E2348C_0642; -.
DR   KO; K02017; -.
DR   OMA; QWLYAQI; -.
DR   BioCyc; ECOL574521:E2348C_RS03450-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015412; F:ATPase-coupled molybdate transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042888; F:molybdenum ion transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR015852; ABC_transpr_ModC.
DR   InterPro; IPR004606; Mo-pterin-bd.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR011868; ModC_ABC_ATP-bd.
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.
PE   3: Inferred from homology;
DR   PRODOM; B7ULN8.
DR   SWISS-2DPAGE; B7ULN8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01705, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00237035};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01705,
KW   ECO:0000256|SAAS:SAAS00236970};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01705,
KW   ECO:0000256|SAAS:SAAS01133279};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01705,
KW   ECO:0000256|SAAS:SAAS01133289};
KW   Molybdenum {ECO:0000256|HAMAP-Rule:MF_01705,
KW   ECO:0000256|SAAS:SAAS00071494};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01705,
KW   ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00452314};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01705,
KW   ECO:0000256|SAAS:SAAS01131829};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01705,
KW   ECO:0000256|SAAS:SAAS00237071}.
FT   DOMAIN        1    229       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      194    352       MODC. {ECO:0000259|PROSITE:PS51241}.
FT   NP_BIND      31     38       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   352 AA;  39071 MW;  34015E8E0EBCAB22 CRC64;
     MLELNFSQTL GNHCLTINET LPANGITAIF GVSGAGKTSL INAISGLTRP QKGRIVLNGR
     VLNDADKGIC LTPEKRRVGY VFQDARLFPH YKVRGNLRYG MAKSMVNQFD 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
//

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