ID A0A0K9H132_9BACI Unreviewed; 261 AA.
AC A0A0K9H132;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Molybdenum ABC transporter substrate-binding protein {ECO:0000313|EMBL:KMY52664.1};
GN ORFNames=AC623_00625 {ECO:0000313|EMBL:KMY52664.1};
OS Bacillus sp. FJAT-27231.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679168 {ECO:0000313|EMBL:KMY52664.1, ECO:0000313|Proteomes:UP000037077};
RN [1] {ECO:0000313|Proteomes:UP000037077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27231 {ECO:0000313|Proteomes:UP000037077};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KMY52664.1}.
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DR EMBL; LFZU01000001; KMY52664.1; -; Genomic_DNA.
DR RefSeq; WP_049659482.1; NZ_LFZU01000001.1.
DR AlphaFoldDB; A0A0K9H132; -.
DR STRING; 1679168.AC623_00625; -.
DR PATRIC; fig|1679168.3.peg.117; -.
DR OrthoDB; 9785015at2; -.
DR Proteomes; UP000037077; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000037077};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..261
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039024529"
FT BINDING 44
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 72
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 154
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 181
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 199
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 261 AA; 28575 MW; 47D02CFFCBB0C5F3 CRC64;
MFKKGWALLF LALLLTAASG CANSGQSASK PDKKTELVIS AAASLTDALD ELQSSFEDEH
PDIDLTFNFG SSGKLAQQIE QGAPADVFLS ASNQDMDKLQ DKNLIQKDSR LEFAKNSLVL
IAKKEQSIPI SSFEEITLKK MDHLAMGEPE SVPAGRYTKE VLEHLNIWES LQNKLVLGSD
VRQVLTYIES GNADLGVVYA SDALTSDKVK VVSKAKSEWH EPIVYPGAIT SHSEHAKAAK
LFLDYLTSTE GKEVLHQYGF N
//
