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Database: UniProt
Entry: A0A1Q9K1V1_9FIRM
LinkDB: A0A1Q9K1V1_9FIRM
Original site: A0A1Q9K1V1_9FIRM 
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
//
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