ID A0A268TPQ5_9HELI Unreviewed; 256 AA.
AC A0A268TPQ5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:PAF46684.1};
GN ORFNames=BKH46_06865 {ECO:0000313|EMBL:PAF46684.1};
OS Helicobacter sp. 12S02634-8.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1476199 {ECO:0000313|EMBL:PAF46684.1, ECO:0000313|Proteomes:UP000216003};
RN [1] {ECO:0000313|EMBL:PAF46684.1, ECO:0000313|Proteomes:UP000216003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12S02634-8 {ECO:0000313|EMBL:PAF46684.1,
RC ECO:0000313|Proteomes:UP000216003};
RX PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT independent niche adaptation followed by diversification in a
RT poikilothermic host.";
RL Sci. Rep. 7:8387-8387(2017).
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:PAF46684.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLAP01000009; PAF46684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268TPQ5; -.
DR Proteomes; UP000216003; 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}.
FT BINDING 66
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 173
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 256 AA; 28171 MW; AA6E65A5F849F57E CRC64;
MLQKGDKTMR KLFVISFLLI GLLFARENGE INVAAAANLA YVMGDIQKEF LTTHPNDKIN
ISYSSSGKAY AQITQGAPID LFISADREFP HKLYTQGKAP QKERVYAQGV LVLWSANPKI
KITSLQTLTL PSITHIAIPN PALAPYGYAA KEALEKTGLG QKIHTKLINA TSISQAHQFV
ATGSAEAGFG ALSLIDKQDK KISYIIIDKS LYSPIEQALI LTNHGKDKEL AKEFEAFILS
PKAKKIFEKY GYIVNE
//