ID A4T1X2_MYCGI Unreviewed; 341 AA.
AC A4T1X2;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Extracellular solute-binding protein, family 1 {ECO:0000313|EMBL:ABP45335.1};
GN OrderedLocusNames=Mflv_2858 {ECO:0000313|EMBL:ABP45335.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP45335.1};
RN [1] {ECO:0000313|EMBL:ABP45335.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP45335.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP45335.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP45335.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000256|ARBA:ARBA00008520}.
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DR EMBL; CP000656; ABP45335.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T1X2; -.
DR STRING; 350054.Mflv_2858; -.
DR KEGG; mgi:Mflv_2858; -.
DR eggNOG; COG1840; Bacteria.
DR HOGENOM; CLU_026974_2_0_11; -.
DR OrthoDB; 9769567at2; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd13543; PBP2_Fbp; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR026045; Ferric-bd.
DR PANTHER; PTHR30006:SF15; IRON-UTILIZATION PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR30006; THIAMINE-BINDING PERIPLASMIC PROTEIN-RELATED; 1.
DR Pfam; PF13343; SBP_bac_6; 1.
DR PIRSF; PIRSF002825; CfbpA; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|PIRSR:PIRSR002825-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR002825-1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..341
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038629184"
FT BINDING 43
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR002825-1"
FT BINDING 91
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR002825-1"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR002825-1"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR002825-1"
SQ SEQUENCE 341 AA; 36852 MW; 29C0DA521E0F8FC6 CRC64;
MSTRRTRWNR IVALIVAGGL AAGLTACSSS EEEDGLLVYN AQHESLTKEW IDAFTKETGI
KVTYRQGGDT ELGNQLIAEG DASPADVFLT ENSPAMAAVE RDGLFTDVDE ATIAQVPPQF
RPATSKWTGV AARTTVFAYD KTKLTEAQLP TSIMDLEKPE WKGRWGAPPV KPDFQAIVAA
MLELTGERAT GQWLAGMKAG AEIYSDNIAT LRAVNDGQVE GGIIYHYYWF RDQSQTKEIS
GNTALHYFRN QDPGAFVSIS GGGILNSSKK KEDAQKFLTF ITSKAGQEVL EKGTSFEYPV
ASGVPANPAL VPLVDLQAPA VNPSNLDAQK VTDLMTKAGL L
//
