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MODA_AZOVI
ID   MODA_AZOVI              Reviewed;         252 AA.
AC   P37734;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Molybdate-binding protein ModA {ECO:0000305};
DE   AltName: Full=Molybdate/tungstate-binding protein ModA {ECO:0000305};
DE   Flags: Precursor;
GN   Name=modA; Synonyms=modB;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DJ35;
RX   PubMed=8384683; DOI=10.1111/j.1365-2958.1993.tb01136.x;
RA   Luque F., Mitchenall L.A., Chapman M., Christine R., Pau R.N.;
RT   "Characterization of genes involved in molybdenum transport in Azotobacter
RT   vinelandii.";
RL   Mol. Microbiol. 7:447-459(1993).
RN   [2]
RP   GENE NAME.
RX   PubMed=7665518; DOI=10.1128/jb.177.18.5294-5302.1995;
RA   Mouncey N.J., Mitchenall L.A., Pau R.N.;
RT   "Mutational analysis of genes of the mod locus involved in molybdenum
RT   transport, homeostasis, and processing in Azotobacter vinelandii.";
RL   J. Bacteriol. 177:5294-5302(1995).
CC   -!- FUNCTION: Involved in the transport of molybdenum into the cell.
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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC       family. {ECO:0000305}.
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DR   EMBL; X69077; CAA48820.1; -; Genomic_DNA.
DR   PIR; S31044; S31044.
DR   RefSeq; WP_012703508.1; NZ_FPKM01000015.1.
DR   AlphaFoldDB; P37734; -.
DR   SMR; P37734; -.
DR   OMA; YGATGQF; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030973; F:molybdate ion binding; ISS:UniProtKB.
DR   GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR   CDD; cd13539; PBP2_AvModA; 1.
DR   InterPro; IPR044084; AvModA-like_subst-bd.
DR   InterPro; IPR005950; ModA.
DR   PIRSF; PIRSF004846; ModA; 1.
DR   TIGRFAMs; TIGR01256; modA; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Molybdenum; Periplasm; Signal; Transport; Tungsten.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..252
FT                   /note="Molybdate-binding protein ModA"
FT                   /id="PRO_0000031826"
FT   BINDING         60
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:P37329"
FT   BINDING         168
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:P37329"
SQ   SEQUENCE   252 AA;  26284 MW;  A655F0086ABEA40C CRC64;
     MSFSLSRLVV ALGAGLLACA AQAAEVQVAV AANFTAPMKD IASQFEKDTG HKVITSFGPT
     GGFYSQIQNG APFEVFLAAD DTTPEKLEKE GGTVAGSRFT YAVGKLVLWS AKPGYVDDQG
     AVLKKNAFKH LSIANPKTAP YGAAAVQVLA KLGLTEATKS KLVEGASIAQ AHQFVATGNA
     ELGFVALSQV YKDGKLTGGS GWNVPGDLYE PIRQDAVILT KGKDNPAAQA LVDYLKGPKA
     TEVIKAYGYG LQ
 
 
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