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Database: UniProt
Entry: A0A2T2YNY2_9BACT
LinkDB: A0A2T2YNY2_9BACT
Original site: A0A2T2YNY2_9BACT 
ID   A0A2T2YNY2_9BACT        Unreviewed;       250 AA.
AC   A0A2T2YNY2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:PSR57215.1};
GN   Name=modA {ECO:0000313|EMBL:PSR57215.1};
GN   ORFNames=AHMF7605_07700 {ECO:0000313|EMBL:PSR57215.1};
OS   Adhaeribacter arboris.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Adhaeribacter.
OX   NCBI_TaxID=2072846 {ECO:0000313|EMBL:PSR57215.1, ECO:0000313|Proteomes:UP000240357};
RN   [1] {ECO:0000313|EMBL:PSR57215.1, ECO:0000313|Proteomes:UP000240357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF7605 {ECO:0000313|EMBL:PSR57215.1,
RC   ECO:0000313|Proteomes:UP000240357};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Adhaeribacter sp. HMF7605 Genome sequencing and assembly.";
RL   Submitted (MAR-2018) 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:PSR57215.1}.
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DR   EMBL; PYFT01000001; PSR57215.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T2YNY2; -.
DR   OrthoDB; 9785015at2; -.
DR   Proteomes; UP000240357; 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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..250
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015741131"
FT   BINDING         57
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         164
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ   SEQUENCE   250 AA;  27655 MW;  F3AE0AD27A88E7DF CRC64;
     MKSLFTWILL FLGLSLVSRA QPVRVAVAAN AQFVIKILQK DFEKKTGVKT EIITGSSGKI
     TAQIKNGAPY DIFLSADMAY PTNLFKSGFG LNAPKVYALG SLIVCSTADL TLENWRQLLT
     TSSINKIALA NPALAPYGQA AREALQHYGI WEKVQPKLVY GESIAQVNTY ITTGAVKIGF
     TSEALIYENP NKNKFKWVRV ENKVYSTMEQ GMVVLSHAKK GNYAHAMQFY AYLSSPAAQQ
     IFRQNGYRVP
//
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