ID Q165A6_ROSDO Unreviewed; 282 AA.
AC Q165A6;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Molybdate ABC transporter, periplasmic molybdate-binding protein {ECO:0000313|EMBL:ABG32437.1};
GN Name=modA {ECO:0000313|EMBL:ABG32437.1};
GN OrderedLocusNames=RD1_2913 {ECO:0000313|EMBL:ABG32437.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG32437.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG32437.1, ECO:0000313|Proteomes:UP000007029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX PubMed=17098896; DOI=10.1128/JB.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000256|ARBA:ARBA00009175}.
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DR EMBL; CP000362; ABG32437.1; -; Genomic_DNA.
DR AlphaFoldDB; Q165A6; -.
DR STRING; 375451.RD1_2913; -.
DR KEGG; rde:RD1_2913; -.
DR eggNOG; COG0725; Bacteria.
DR HOGENOM; CLU_065520_3_0_5; -.
DR Proteomes; UP000007029; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR005950; ModA.
DR NCBIfam; TIGR01256; modA; 1.
DR PANTHER; PTHR30632; MOLYBDATE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR30632:SF17; MOLYBDATE-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.
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:UP000007029};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT BINDING 60
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 87
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 172
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 199
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 217
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 282 AA; 29538 MW; 4D3A1FC0C5B2F58E CRC64;
MTPIVPPQRG KPLAPRLSLR DNGPMSDVLR RILFILASVL CATACLPAAA GQITVFAAAS
LKEAIDEISA DFTRATGVEV AASYAGSSAL ARQIEFGAPA DVFLSASTEW MDHLEHNNRI
EPTTRFDLVG NRLVLIGPAA QTAAFEISAN TNLLHMLAGG RLAMALTDAV PAGIYGKTAL
QRLGLWEGVA PMVAQTDNVR AALSLVSLGA APLGIVYATD AQADQNVSLR ATFPPHTHPP
IIYPVALVKG AKSPQAQAFL DYLTGDAADK VFADLGFLVG AE
//
