ID A0A0Q6U8L1_9CAUL Unreviewed; 252 AA.
AC A0A0Q6U8L1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:KQV62545.1};
GN ORFNames=ASC62_03145 {ECO:0000313|EMBL:KQV62545.1};
OS Caulobacter sp. Root342.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1736519 {ECO:0000313|EMBL:KQV62545.1, ECO:0000313|Proteomes:UP000051656};
RN [1] {ECO:0000313|EMBL:KQV62545.1, ECO:0000313|Proteomes:UP000051656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root342 {ECO:0000313|EMBL:KQV62545.1,
RC ECO:0000313|Proteomes:UP000051656};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV62545.1, ECO:0000313|Proteomes:UP000051656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root342 {ECO:0000313|EMBL:KQV62545.1,
RC ECO:0000313|Proteomes:UP000051656};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000256|ARBA:ARBA00009175}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQV62545.1}.
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DR EMBL; LMDD01000001; KQV62545.1; -; Genomic_DNA.
DR RefSeq; WP_056053079.1; NZ_LMDD01000001.1.
DR AlphaFoldDB; A0A0Q6U8L1; -.
DR STRING; 1736519.ASC62_03145; -.
DR OrthoDB; 9785015at2; -.
DR Proteomes; UP000051656; Unassembled WGS sequence.
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.
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..252
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006292816"
FT BINDING 63
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 171
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 252 AA; 26461 MW; 2C71D4A86DA50685 CRC64;
MIARRPILIA ALSGALLLTL GGGAQAGETK VAVAANFTEA AREIATKFKA KTGHDATLSF
GSSGQFYTQI ANGAPYEVFL SADVERPQRA EAEGLAVPGS RFTYATGRLV LWSRTPGLVD
GKGAVLAKGK FEKLAIADPK AAPYGQAAVE TLTKLKLYDA LKPKIVTGAS ISQAYQYVQT
GAAELGFVAL SQVVDEKGGS RWLAPASDHS PIEQQAVLLK TGANSAAAKA FLKFLKSGEA
KAIIKRYGYE VR
//
