ID A0A268TUB8_9HELI Unreviewed; 245 AA.
AC A0A268TUB8;
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:PAF47946.1};
GN ORFNames=BKH41_06690 {ECO:0000313|EMBL:PAF47946.1};
OS Helicobacter sp. 12S02232-10.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1476197 {ECO:0000313|EMBL:PAF47946.1, ECO:0000313|Proteomes:UP000216724};
RN [1] {ECO:0000313|EMBL:PAF47946.1, ECO:0000313|Proteomes:UP000216724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12S02232-10 {ECO:0000313|EMBL:PAF47946.1,
RC ECO:0000313|Proteomes:UP000216724};
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:PAF47946.1}.
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DR EMBL; MLAQ01000007; PAF47946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268TUB8; -.
DR OrthoDB; 9785015at2; -.
DR Proteomes; UP000216724; 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..245
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012402335"
FT BINDING 55
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 162
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 245 AA; 27160 MW; 4E37D0FEE91533DF CRC64;
MRKLFFLCVL FVVASFGREI NVAAAANLAH TLQEIQKEFL NTHPQDKINI SYSSSGKAYA
QISQGAPIDL FVSADREFPH KLYEEGKTPQ EERIYAQGVL VLWSANPKIK ITSLEMLADK
NIVHIAIPNP KLAPYGRAAK ESLEKTRLEG KIKSKLINAV SISQAHQFVA SGNAQAGFGA
LSLIDKKDKN ISYIIVDKSL YSPIDQALVL TNYGKDNELA KEFEAFILSP NAKAIFKKFG
YIVNE
//
