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Database: UniProt
Entry: B1W141_STRGG
LinkDB: B1W141_STRGG
Original site: B1W141_STRGG 
ID   B1W141_STRGG            Unreviewed;       320 AA.
AC   B1W141;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Putative arginine/ornithine binding protein {ECO:0000313|EMBL:BAG19066.1};
GN   OrderedLocusNames=SGR_2237 {ECO:0000313|EMBL:BAG19066.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG19066.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG19066.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC       {ECO:0000256|ARBA:ARBA00010333}.
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DR   EMBL; AP009493; BAG19066.1; -; Genomic_DNA.
DR   RefSeq; WP_003966334.1; NC_010572.1.
DR   AlphaFoldDB; B1W141; -.
DR   GeneID; 6213155; -.
DR   KEGG; sgr:SGR_2237; -.
DR   PATRIC; fig|455632.4.peg.2277; -.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_019602_18_1_11; -.
DR   Proteomes; UP000001685; Chromosome.
DR   CDD; cd01004; PBP2_MidA_like; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR35936:SF27; L-ARGININE-BINDING PROTEIN; 1.
DR   PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00062; PBPb; 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|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..320
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038965504"
FT   DOMAIN          68..308
FT                   /note="Solute-binding protein family 3/N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00062"
FT   REGION          34..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   320 AA;  33311 MW;  B0A89AC488763F6C CRC64;
     MTASTTRRTT AKSRIAAIGA IAVAGTLLLT ACGDQTDSSS QESGSGKETK SGAPLFSKLP
     EKYQKSGVIK VGTNAEYAPM ESVENGKIVG VDPDIAEALG KQLGVRFEFT SGSFDGLITA
     LNSGRHDIAM SSITDNKQRQ EGLDDSGKKL GEGVDFVDYF LAGTAVYTKK GNPQNIKSIE
     DLCGKPAAVQ RGTTYEEALK KQSKACTDGG EKAIKIESFE NDTEAQTRVK SGGSVAGVND
     YPVAVDLARK ADGGKAFEVV GEQVDAGPFG IAVKKDNTGL RDALKEAVDA IIADGSYQKV
     LDKWGAGTGA IDKAAINGGK
//
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