ARGT_SALTY
ID ARGT_SALTY Reviewed; 260 AA.
AC P02911;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Lysine/arginine/ornithine-binding periplasmic protein;
DE Short=LAO-binding protein;
DE Flags: Precursor;
GN Name=argT; OrderedLocusNames=STM2355;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=6273842; DOI=10.1073/pnas.78.10.6038;
RA Higgins C.F., Ames G.F.-L.;
RT "Two periplasmic transport proteins which interact with a common membrane
RT receptor show extensive homology: complete nucleotide sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:6038-6042(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND SUBUNIT.
RX PubMed=24021237; DOI=10.1016/j.bbamem.2013.08.024;
RA Heuveling J., Frochaux V., Ziomkowska J., Wawrzinek R., Wessig P.,
RA Herrmann A., Schneider E.;
RT "Conformational changes of the bacterial type I ATP-binding cassette
RT importer HisQMP2 at distinct steps of the catalytic cycle.";
RL Biochim. Biophys. Acta 1838:106-116(2014).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=1748660; DOI=10.1016/s0021-9258(18)54367-2;
RA Kang C.-H., Shin W.-C., Yamagata Y., Gokcen S., Ames G.F.-L., Kim S.-H.;
RT "Crystal structure of the lysine-, arginine-, ornithine-binding protein
RT (LAO) from Salmonella typhimurium at 2.7-A resolution.";
RL J. Biol. Chem. 266:23893-23899(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8496186; DOI=10.1016/s0021-9258(18)82131-7;
RA Oh B.-H., Pandit J., Kang C.-H., Nikaido K., Gokcen S., Ames G.F.-L.,
RA Kim S.-H.;
RT "Three-dimensional structures of the periplasmic lysine/arginine/ornithine-
RT binding protein with and without a ligand.";
RL J. Biol. Chem. 268:11348-11355(1993).
RN [6]
RP ERRATUM OF PUBMED:8496186.
RA Oh B.-H., Pandit J., Kang C.-H., Nikaido K., Gokcen S., Ames G.F.-L.,
RA Kim S.-H.;
RL J. Biol. Chem. 268:17648-17649(1993).
CC -!- FUNCTION: Part of an ABC transporter involved in lysine, arginine and
CC ornithine transport. Stimulates ATPase activity of HisP.
CC {ECO:0000269|PubMed:24021237, ECO:0000269|PubMed:6273842}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HisP),
CC two transmembrane proteins (HisM and HisQ) and a solute-binding protein
CC (ArgT). {ECO:0000269|PubMed:24021237}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:6273842}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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DR EMBL; V01368; CAA24651.1; -; Genomic_DNA.
DR EMBL; J01805; AAA75577.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21256.1; -; Genomic_DNA.
DR PIR; A03408; JKEBT.
DR RefSeq; NP_461297.1; NC_003197.2.
DR RefSeq; WP_000754423.1; NC_003197.2.
DR PDB; 1LAF; X-ray; 2.06 A; E=23-260.
DR PDB; 1LAG; X-ray; 2.06 A; E=23-260.
DR PDB; 1LAH; X-ray; 2.06 A; E=23-260.
DR PDB; 1LST; X-ray; 1.80 A; A=23-260.
DR PDB; 2LAO; X-ray; 1.90 A; A=23-260.
DR PDB; 5OWF; X-ray; 1.91 A; A=23-260.
DR PDB; 6FT2; X-ray; 1.25 A; A=23-260.
DR PDB; 6MKU; X-ray; 1.73 A; E=23-260.
DR PDB; 6MKW; X-ray; 2.32 A; A=24-260.
DR PDB; 6MKX; X-ray; 2.28 A; A=23-260.
DR PDB; 6ML0; X-ray; 1.68 A; A=23-260.
DR PDB; 6ML9; X-ray; 1.69 A; E=23-260.
DR PDB; 6MLA; X-ray; 1.58 A; E=23-260.
DR PDB; 6MLD; X-ray; 1.66 A; A=23-260.
DR PDB; 6MLE; X-ray; 1.86 A; E=23-260.
DR PDB; 6MLG; X-ray; 1.89 A; E=23-260.
DR PDB; 6MLI; X-ray; 1.88 A; E=23-260.
DR PDB; 6MLJ; X-ray; 1.60 A; A/B=24-260.
DR PDB; 6MLN; X-ray; 1.72 A; E=23-260.
DR PDB; 6MLO; X-ray; 1.72 A; E=23-260.
DR PDB; 6MLP; X-ray; 1.49 A; E=23-260.
DR PDB; 6MLV; X-ray; 2.08 A; A=23-260.
DR PDB; 6XKS; X-ray; 2.40 A; A/B/C=23-260.
DR PDBsum; 1LAF; -.
DR PDBsum; 1LAG; -.
DR PDBsum; 1LAH; -.
DR PDBsum; 1LST; -.
DR PDBsum; 2LAO; -.
DR PDBsum; 5OWF; -.
DR PDBsum; 6FT2; -.
DR PDBsum; 6MKU; -.
DR PDBsum; 6MKW; -.
DR PDBsum; 6MKX; -.
DR PDBsum; 6ML0; -.
DR PDBsum; 6ML9; -.
DR PDBsum; 6MLA; -.
DR PDBsum; 6MLD; -.
DR PDBsum; 6MLE; -.
DR PDBsum; 6MLG; -.
DR PDBsum; 6MLI; -.
DR PDBsum; 6MLJ; -.
DR PDBsum; 6MLN; -.
DR PDBsum; 6MLO; -.
DR PDBsum; 6MLP; -.
DR PDBsum; 6MLV; -.
DR PDBsum; 6XKS; -.
DR AlphaFoldDB; P02911; -.
DR SMR; P02911; -.
DR STRING; 99287.STM2355; -.
DR PaxDb; P02911; -.
DR PRIDE; P02911; -.
DR EnsemblBacteria; AAL21256; AAL21256; STM2355.
DR GeneID; 1253877; -.
DR KEGG; stm:STM2355; -.
DR PATRIC; fig|99287.12.peg.2492; -.
DR HOGENOM; CLU_019602_18_0_6; -.
DR OMA; LYPTSYH; -.
DR PhylomeDB; P02911; -.
DR BioCyc; SENT99287:STM2355-MON; -.
DR EvolutionaryTrace; P02911; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR005768; Lys_Arg_Orn-bd.
DR InterPro; IPR018313; SBP_3_CS.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR TIGRFAMs; TIGR01096; 3A0103s03R; 1.
DR PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Disulfide bond; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT CHAIN 23..260
FT /note="Lysine/arginine/ornithine-binding periplasmic
FT protein"
FT /id="PRO_0000031750"
FT DISULFID 60..67
FT CONFLICT 124
FT /note="I -> V (in Ref. 1; CAA24651/AAA75577)"
FT /evidence="ECO:0000305"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6MLP"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5OWF"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:6FT2"
FT TURN 128..133
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:6FT2"
FT TURN 152..156
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:6FT2"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6FT2"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:6FT2"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:6FT2"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:6FT2"
SQ SEQUENCE 260 AA; 28200 MW; B996DE523F5F80A5 CRC64;
MKKTVLALSL LIGLGATAAS YAALPQTVRI GTDTTYAPFS SKDAKGEFIG FDIDLGNEMC
KRMQVKCTWV ASDFDALIPS LKAKKIDAII SSLSITDKRQ QEIAFSDKLY AADSRLIAAK
GSPIQPTLES LKGKHVGVLQ GSTQEAYAND NWRTKGVDVV AYANQDLIYS DLTAGRLDAA
LQDEVAASEG FLKQPAGKEY AFAGPSVKDK KYFGDGTGVG LRKDDTELKA AFDKALTELR
QDGTYDKMAK KYFDFNVYGD
