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Database: UniProt
Entry: A0A139WUS2_9CYAN
LinkDB: A0A139WUS2_9CYAN
Original site: A0A139WUS2_9CYAN 
ID   A0A139WUS2_9CYAN        Unreviewed;       258 AA.
AC   A0A139WUS2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Molybdate ABC transporter substrate-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=WA1_41195 {ECO:0000313|EMBL:KYC36157.1};
OS   Scytonema hofmannii PCC 7110.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC36157.1, ECO:0000313|Proteomes:UP000076925};
RN   [1] {ECO:0000313|EMBL:KYC36157.1, ECO:0000313|Proteomes:UP000076925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC36157.1,
RC   ECO:0000313|Proteomes:UP000076925};
RX   PubMed=23221676; DOI=10.1093/gbe/evs117;
RA   Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA   Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA   Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT   "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT   of oxygenic photosynthesis from prokaryotes to plastids.";
RL   Genome Biol. Evol. 5:31-44(2013).
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:KYC36157.1}.
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DR   EMBL; ANNX02000047; KYC36157.1; -; Genomic_DNA.
DR   RefSeq; WP_017742853.1; NZ_KQ976354.1.
DR   AlphaFoldDB; A0A139WUS2; -.
DR   STRING; 128403.WA1_41195; -.
DR   OrthoDB; 482811at2; -.
DR   Proteomes; UP000076925; 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.
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:UP000076925};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   BINDING         148
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT   BINDING         176
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ   SEQUENCE   258 AA;  28930 MW;  D517FD347DCA3AB1 CRC64;
     MKRRKFLILT SSITILYLGL NSCNTHQTKP VALTISAAAV FRDAMVEVGR LYTEKQPNIL
     VNYNITGGGV LKKQIELGAP VDVYLPASVR PMNELQKKGF ILEDSRQNFM KNEIVLISLN
     NFTGSSNFQD ILNNKVKRIA LGTENIDAGI YAKQILDFFK IYDQVKSKGI FEEQDVQQVL
     KYVETGHADV GITFLTEAKR SRKVKILAIS PEGSHAPVIS TIAVVKNSKH IAEAREFINF
     LKSDRAISIF EKFGFMKI
//
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