ID A0A1Q9K1V1_9FIRM Unreviewed; 267 AA.
AC A0A1Q9K1V1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:OLR62546.1};
GN ORFNames=BHF69_07610 {ECO:0000313|EMBL:OLR62546.1};
OS Anaerostipes sp. 992a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=1261637 {ECO:0000313|EMBL:OLR62546.1, ECO:0000313|Proteomes:UP000187371};
RN [1] {ECO:0000313|EMBL:OLR62546.1, ECO:0000313|Proteomes:UP000187371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=992a {ECO:0000313|EMBL:OLR62546.1,
RC ECO:0000313|Proteomes:UP000187371};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(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:OLR62546.1}.
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DR EMBL; MJIG01000004; OLR62546.1; -; Genomic_DNA.
DR RefSeq; WP_075670439.1; NZ_MJIG01000004.1.
DR AlphaFoldDB; A0A1Q9K1V1; -.
DR STRING; 1261637.BHF69_07610; -.
DR OrthoDB; 9785015at2; -.
DR Proteomes; UP000187371; 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; cd13537; PBP2_YvgL_like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR005950; ModA.
DR InterPro; IPR041879; YvgL-like_PBP2.
DR NCBIfam; TIGR01256; modA; 1.
DR PANTHER; PTHR30632:SF0; ABC TRANSPORTER SUBSTRATE-BINDING LIPOPROTEIN YVGL-RELATED; 1.
DR PANTHER; PTHR30632; MOLYBDATE-BINDING PERIPLASMIC 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 Reference proteome {ECO:0000313|Proteomes:UP000187371};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..267
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038796238"
FT BINDING 46
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 74
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 182
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 200
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 267 AA; 29567 MW; EAD9B36A5DD40856 CRC64;
MKRLKKLIAL LCVLLMGFAL TACGGSKESD TKTENKTEIH ILAAASMTDV LNELGKSYEK
EHPDVRLTFT YDSSGTLQTQ IEEGAPADVF LSAATQQMNA LKEQGLMEED SIIRLLENEV
VLIKPEGSDL DIQTFEDVAT DKVEMVAIGN SDVPVGQYTE TIYKNMGLWK KIKEKANLGT
NVRQVLDWVA TKNVDCGIVY ATDAAIEDRV EVVCAAPADS CEPAIYPAGV VKATEHEEEA
QEFLDFLKTD EAKKAFEKYK FTYIYSE
//