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Database: UniProt
Entry: A0A0T2L0J2_9MICO
LinkDB: A0A0T2L0J2_9MICO
Original site: A0A0T2L0J2_9MICO 
ID   A0A0T2L0J2_9MICO        Unreviewed;       331 AA.
AC   A0A0T2L0J2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Solute-binding protein family 3/N-terminal domain-containing protein {ECO:0000259|SMART:SM00062};
GN   ORFNames=ASD65_14170 {ECO:0000313|EMBL:KRA25439.1};
OS   Microbacterium sp. Root61.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA25439.1, ECO:0000313|Proteomes:UP000051216};
RN   [1] {ECO:0000313|EMBL:KRA25439.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA25439.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA25439.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA25439.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRA25439.1}.
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DR   EMBL; LMGU01000001; KRA25439.1; -; Genomic_DNA.
DR   RefSeq; WP_056223691.1; NZ_LMGU01000001.1.
DR   AlphaFoldDB; A0A0T2L0J2; -.
DR   STRING; 1736570.ASD65_14170; -.
DR   OrthoDB; 7808807at2; -.
DR   Proteomes; UP000051216; Unassembled WGS sequence.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR027939; NMT1/THI5.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   InterPro; IPR015168; SsuA/THI5.
DR   PANTHER; PTHR31528; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1.
DR   PANTHER; PTHR31528:SF3; THIAMINE BIOSYNTHESIS PROTEIN HI_0357-RELATED; 1.
DR   Pfam; PF09084; NMT1; 1.
DR   SMART; SM00062; PBPb; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051216};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..331
FT                   /note="Solute-binding protein family 3/N-terminal domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038675113"
FT   DOMAIN          50..265
FT                   /note="Solute-binding protein family 3/N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00062"
SQ   SEQUENCE   331 AA;  34683 MW;  807822911CBF4674 CRC64;
     MKRSAKMLLG LGAVVALALT ACSSGTPESA ESTPAADGEL QTVNIVGVPV VDMAALYVGE
     DQGFFAEEGL ELNIEFGQGT AAMIPALING QYDIQYGGSV NMLQAVDAEL PVVAIAAGGR
     TTGVQGEDHG GLLVLEDSPI QTAADLEGKT VAVNALRGLH EVALWASIRK AGGDPTKVNF
     VEMALPDMGA ALESGQIDAA STSEPFLGVL QGEGARLVTS LYVDADPDFV TALYFVTAEK
     AEKDRDMIER FNRALEKSFA YSTENPDAVR AQLGNFTQID PALIETMILT NFKWGLTDAD
     LLLIANLAAD ANSLEDPEAA AERAAAFIDS E
//
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