ID   A0A1M3EWT1_9CELL        Unreviewed;       267 AA.
AC   A0A1M3EWT1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0000313|EMBL:OJV76703.1};
GN   ORFNames=BGO37_10260 {ECO:0000313|EMBL:OJV76703.1};
OS   Cellulomonas sp. 73-92.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895740 {ECO:0000313|EMBL:OJV76703.1, ECO:0000313|Proteomes:UP000184539};
RN   [1] {ECO:0000313|EMBL:OJV76703.1, ECO:0000313|Proteomes:UP000184539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-92 {ECO:0000313|EMBL:OJV76703.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJV76703.1}.
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DR   EMBL; MKTH01000024; OJV76703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3EWT1; -.
DR   STRING; 1895740.BGO37_10260; -.
DR   Proteomes; UP000184539; 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   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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..267
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012679818"
FT   BINDING         56
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         84
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         184
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         202
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ   SEQUENCE   267 AA;  26119 MW;  D19EE295C4F3E861 CRC64;
     MAGVLRSAAV AVAVVLALAA CASTPAARPT ASSGTLDPVT TTPALTGRLT VFAAASLQGT
     FTQLGDQMMA AHPGLTVTFS FGSSGTLTQQ LLAGAPADVY ASASTTTMAD AASVVGTPTV
     FTHNSLVIVV PKGNPAGVTG LADFARPALK IALCDPSAPC GAAAKQVFAK AGITPALDTL
     GQDVKATLAL VTAGEVDAAL VYKTDAIAAG PAVQAIAVPQ ADAVVNDYPI ALVKGTTNPA
     AAQAFVDEVL SPAGRHVLAA AGFDPAG
//