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Database: UniProt
Entry: A0A1Q7W9D2_9ACTN
LinkDB: A0A1Q7W9D2_9ACTN
Original site: A0A1Q7W9D2_9ACTN 
ID   A0A1Q7W9D2_9ACTN        Unreviewed;       544 AA.
AC   A0A1Q7W9D2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Solute-binding protein family 5 domain-containing protein {ECO:0000259|Pfam:PF00496};
GN   ORFNames=AUG49_05465 {ECO:0000313|EMBL:OLE27375.1};
OS   Catenulispora sp. 13_1_20CM_3_70_7.
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=1805055 {ECO:0000313|EMBL:OLE27375.1, ECO:0000313|Proteomes:UP000186605};
RN   [1] {ECO:0000313|EMBL:OLE27375.1, ECO:0000313|Proteomes:UP000186605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {ECO:0000256|ARBA:ARBA00005695}.
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:OLE27375.1}.
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DR   EMBL; MNJN01000086; OLE27375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7W9D2; -.
DR   Proteomes; UP000186605; Unassembled WGS sequence.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290:SF88; OLIGOPEPTIDE-BINDING PROTEIN APPA; 1.
DR   PANTHER; PTHR30290; PERIPLASMIC BINDING COMPONENT OF ABC TRANSPORTER; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..544
FT                   /note="Solute-binding protein family 5 domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012321897"
FT   DOMAIN          118..437
FT                   /note="Solute-binding protein family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00496"
FT   REGION          26..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  58002 MW;  622E0AC3D5ACAF0C CRC64;
     MNRHSKLLGG VALAASVALA ASACSSSKSK SSPSTKPTGN VTTLPSGANS SAEGFNAAVN
     GFVRPTDKQG GTMTLVNRSD WDSPDTGNQY DAFAWAFDGN YARSMMAYAQ KPGVEGTKVV
     PDLAQAAGVV SDGGLTWTYK IKTGVKYSDG TVVKAADVKY AIERSNWGQD VLQNGPNYFT
     NFVKDDTKYQ GPYKDTNPAD GVSGIQTPDD STIVFHLKQP FADFDYLMAI PGSAPVPRSA
     DKGAEYFKSY LATGQYKIDS YKPGVEMDLS PNPSFDPSTD PDKLHVLRAS KIVVKVKQDK
     STIDDQLFNG SADGDLTGVG VQAAGQAKVM GDPKLKADAD SAYANSESYF AINGTMKPFD
     NLDCRQAVEW ITDKNTMQTQ LGGPIAGGDI ATTAQPPTVP GWVKEDQYAT TDHKGDATKA
     KASLAKCQSA EPDQFNFFFK QKTPRSTRSP STSTTRTSRA TGSTRRPTRW PSASPSGAGT
     SRPATATCTA SSPAAPSTNR ATTSCPGWTT RPWTRASKRL WPRPTRPSVT PTTPRSTTRS
     CPTR
//
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