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Database: UniProt
Entry: A0A241WIR1_9GAMM
LinkDB: A0A241WIR1_9GAMM
Original site: A0A241WIR1_9GAMM 
ID   A0A241WIR1_9GAMM        Unreviewed;       252 AA.
AC   A0A241WIR1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:OTG93868.1};
GN   ORFNames=B9T35_09215 {ECO:0000313|EMBL:OTG93868.1};
OS   Acinetobacter sp. ANC 3832.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1977874 {ECO:0000313|EMBL:OTG93868.1, ECO:0000313|Proteomes:UP000194704};
RN   [1] {ECO:0000313|EMBL:OTG93868.1, ECO:0000313|Proteomes:UP000194704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3832 {ECO:0000313|EMBL:OTG93868.1,
RC   ECO:0000313|Proteomes:UP000194704};
RA   Nemec A., Radolfova-Krizova L.;
RT   "High diversity of culturable Acinetobacter species in natural soil and
RT   water ecosystems.";
RL   Submitted (APR-2017) 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:OTG93868.1}.
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DR   EMBL; NEGJ01000005; OTG93868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A241WIR1; -.
DR   STRING; 1977874.B9T35_09215; -.
DR   OrthoDB; 9785015at2; -.
DR   Proteomes; UP000194704; Unassembled WGS sequence.
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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..252
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011308408"
FT   BINDING         29
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         57
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         141
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         168
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         186
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ   SEQUENCE   252 AA;  27756 MW;  EE58401648E933C3 CRC64;
     MKNLMIGAVL FSLCNLSQAE TVKVYAAASL TNAISDIAVI YEKQHPQTDI VPVFGASSAL
     AKQIEAGAKS DLFFSADVDW MNYLIKKQMI TENKSKALLS NQLVLISLKN LNIAFKAQPN
     FNFAQSFKGH VCTGQMESVP AGKYAKQSLI KLNWLDSLKG RIVGTDDVRS ALAFVERGEC
     DVGIVYKTDA LISKKVKVIG IFPENSHHPI LYPLALTQQG EKNADAVQFE KFVKSSPQAK
     IIFQKYGFSM NQ
//
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