ID A0A1Q7T750_9CHLR Unreviewed; 276 AA.
AC A0A1Q7T750;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:OLD84344.1};
GN ORFNames=AUG54_00890 {ECO:0000313|EMBL:OLD84344.1};
OS Ktedonobacter sp. 13_1_20CM_4_53_7.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805226 {ECO:0000313|EMBL:OLD84344.1, ECO:0000313|Proteomes:UP000186099};
RN [1] {ECO:0000313|EMBL:OLD84344.1, ECO:0000313|Proteomes:UP000186099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD84344.1}.
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DR EMBL; MNIQ01000057; OLD84344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7T750; -.
DR Proteomes; UP000186099; 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 CDD; cd13538; PBP2_ModA_like_1; 1.
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:SF0; SULFATE-BINDING PROTEIN; 1.
DR Pfam; PF13531; SBP_bac_11; 1.
DR PIRSF; PIRSF004846; ModA; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..276
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013067637"
FT BINDING 49
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 77
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 155
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 191
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 209
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 276 AA; 29298 MW; C4FE3EB20FC60953 CRC64;
MRRSRHALML FILLCTLFLA ACGGSTSSTT STATTAPAVT ILNVFAAASL KESFNVIAAK
YTRAHPNITI KLNFAGSQIL EQQVASGAPA DVFASADQTT MQKAVDAGLV GNSQVFVKNR
LTVIIPAANP GNINTLKDLS RKGVKIDIGA PAVPAGKYSL QVLAKMAQSS NYGPAYENAV
KANFVSQETD VKAVVNKVQL GEVDAGFVYV TDVTAAVSNK IKMIDIPDNF NVIAQYPIAV
TKSSAHSNDA RAFVQYILSP EGQAVLQQYH FIAFNP
//
