ID B1Y6B9_LEPCP Unreviewed; 253 AA.
AC B1Y6B9;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Molybdenum ABC transporter, periplasmic molybdate-binding protein {ECO:0000313|EMBL:ACB33624.1};
DE Flags: Precursor;
GN OrderedLocusNames=Lcho_1356 {ECO:0000313|EMBL:ACB33624.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB33624.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB33624.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000256|ARBA:ARBA00009175}.
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DR EMBL; CP001013; ACB33624.1; -; Genomic_DNA.
DR RefSeq; WP_012346386.1; NC_010524.1.
DR AlphaFoldDB; B1Y6B9; -.
DR STRING; 395495.Lcho_1356; -.
DR KEGG; lch:Lcho_1356; -.
DR eggNOG; COG0725; Bacteria.
DR HOGENOM; CLU_065520_1_0_4; -.
DR OrthoDB; 9785015at2; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030973; F:molybdate ion binding; IEA:InterPro.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR CDD; cd13539; PBP2_AvModA; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR044084; AvModA-like_subst-bd.
DR InterPro; IPR005950; ModA.
DR NCBIfam; TIGR01256; modA; 1.
DR PANTHER; PTHR30632; MOLYBDATE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR30632:SF14; TUNGSTATE_MOLYBDATE_CHROMATE-BINDING PROTEIN MODA; 1.
DR Pfam; PF13531; SBP_bac_11; 1.
DR PIRSF; PIRSF004846; ModA; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004846-1};
KW Molybdenum {ECO:0000256|PIRSR:PIRSR004846-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..253
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002773384"
FT BINDING 62
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 170
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 253 AA; 26227 MW; 0E98A729DCBEB2F1 CRC64;
MRRINWITGL AMAIGLGCSA GLANAGEVQV AVAANFVGPL AQIGAAFTAA TGHQLVVSSG
ATGRFYSQIK AGAPFEVLIA ADDETPKKLI AENLAVAGSQ FTYAIGQLVL WSARPGLVDA
QGQVLSSQGF AHLAIANPKL APYGAAALEV LRARGLHDAL APRLVTAESI AQAYQFVFTG
NADLGFVALS QVLVPGKPVP GSHWRVPASL HAPIRQDAVL LKAGDKNLAA RALLDYLRSA
PARAVIEAYG YSH
//
