ID A0A1Q5MT64_9ACTN Unreviewed; 271 AA.
AC A0A1Q5MT64;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=ABC transporter substrate-binding protein {ECO:0000313|EMBL:OKK17493.1};
GN ORFNames=AMK16_21990 {ECO:0000313|EMBL:OKK17493.1};
OS Streptomyces sp. CB00455.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK17493.1, ECO:0000313|Proteomes:UP000185643};
RN [1] {ECO:0000313|EMBL:OKK17493.1, ECO:0000313|Proteomes:UP000185643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00455 {ECO:0000313|EMBL:OKK17493.1,
RC ECO:0000313|Proteomes:UP000185643};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(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:OKK17493.1}.
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DR EMBL; LIVQ01000005; OKK17493.1; -; Genomic_DNA.
DR RefSeq; WP_073918437.1; NZ_LIVQ01000005.1.
DR AlphaFoldDB; A0A1Q5MT64; -.
DR STRING; 1703927.AMK16_21990; -.
DR OrthoDB; 9785015at2; -.
DR Proteomes; UP000185643; 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.
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:UP000185643};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..271
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013044332"
FT BINDING 61
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 89
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 189
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 207
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 271 AA; 27679 MW; 361BBF82C010CE3E CRC64;
MYAIPHRRRA AAAALTAALL VPLAACGSDD EQSAAAPSAG ASSPASAAPE AANLTVLAAS
SLTDAFKTAG AAYEKAHPGT RVTFSFAGSQ ELAAQVKQGA PADALVTADT RTMDGLRSET
GEATVIAKNR LVIATGKGNP FKIDELKDLA DTKVKVVLAA PEVPVGRYGK EILDKQGVTV
KPVSQEPNVR AVLGKVELGE ADAGLVYKTD SAKSGDKVVA VDIPDDQNAV ASYPAAALKQ
SKNAEAAAAF VAWLSSPEAQ KILQDAGFQQ A
//
