PHNS_SALTY
ID PHNS_SALTY Reviewed; 337 AA.
AC P96062; Q7CR31;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative 2-aminoethylphosphonate-binding periplasmic protein;
DE Flags: Precursor;
GN Name=phnS; OrderedLocusNames=STM0429;
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].
RC STRAIN=LT2;
RA Metcalf W.W., Jiang W., Wanner B.L.;
RT "Molecular genetic analysis of the Salmonella typhimurium LT2 phnXWRSTUV
RT locus required for 2-aminoethylphosphonate transport and metabolism.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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 CLONING, AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=7592415; DOI=10.1128/jb.177.22.6411-6421.1995;
RA Jiang W., Metcalf W.W., Lee K.-S., Wanner B.L.;
RT "Molecular cloning, mapping, and regulation of Pho regulon genes for
RT phosphonate breakdown by the phosphonatase pathway of Salmonella
RT typhimurium LT2.";
RL J. Bacteriol. 177:6411-6421(1995).
CC -!- FUNCTION: Probably part of the PhnSTUV complex (TC 3.A.1.11.5) involved
CC in 2-aminoethylphosphonate import.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- INDUCTION: Induced when inorganic phosphate is limiting; this is
CC controlled by PhoB. {ECO:0000269|PubMed:7592415}.
CC -!- MISCELLANEOUS: Maps to a phosphate-starvation-inducible locus
CC previously known as psiC.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; U69493; AAB39644.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19383.1; -; Genomic_DNA.
DR PIR; T46949; T46949.
DR RefSeq; NP_459424.1; NC_003197.2.
DR RefSeq; WP_000778012.1; NC_003197.2.
DR PDB; 4R6Y; X-ray; 1.22 A; A=22-337.
DR PDBsum; 4R6Y; -.
DR AlphaFoldDB; P96062; -.
DR SMR; P96062; -.
DR STRING; 99287.STM0429; -.
DR TCDB; 3.A.1.11.5; the atp-binding cassette (abc) superfamily.
DR PaxDb; P96062; -.
DR EnsemblBacteria; AAL19383; AAL19383; STM0429.
DR GeneID; 1251948; -.
DR KEGG; stm:STM0429; -.
DR PATRIC; fig|99287.12.peg.458; -.
DR HOGENOM; CLU_026974_3_2_6; -.
DR OMA; WHKVTDS; -.
DR PhylomeDB; P96062; -.
DR BioCyc; SENT99287:STM0429-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0030975; F:thiamine binding; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0015888; P:thiamine transport; IBA:GO_Central.
DR InterPro; IPR017637; AminoethylPonate_ABC-bd.
DR InterPro; IPR006059; SBP.
DR Pfam; PF01547; SBP_bac_1; 1.
DR TIGRFAMs; TIGR03227; PhnS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..337
FT /note="Putative 2-aminoethylphosphonate-binding periplasmic
FT protein"
FT /id="PRO_0000287400"
FT STRAND 23..33
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:4R6Y"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:4R6Y"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4R6Y"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:4R6Y"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:4R6Y"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:4R6Y"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4R6Y"
FT HELIX 316..335
FT /evidence="ECO:0007829|PDB:4R6Y"
SQ SEQUENCE 337 AA; 36547 MW; 9AA2BDC6177C37EA CRC64;
MKLSRLALLS VFALASAPSW AESVVTVYSI DGLHDGDNSW YQVQFDAFTK ATGITVRYVE
GGGGVVVERL AKERTNPQAD VLVTAPPFIQ RAAAEKLLAN FNTDTASAIP DANNLYSPLV
KNYLSFIYNS KLLKTAPASW QDLLDGKFKN KLQYSTPGQA ADGTAVMLQA FHSFGSKDAG
FAYLGKLQAN NVGPSASTGK LTALVNKGEI YVANGDLQMN LAQMERNPNV KIFWPANDKG
ERSALAIPYV IGLVQGAPQS ENGKKLINFL LSKEAQTRVS ELSWGMPVRS DVTPSDEHYK
AATAALEGVQ SWQPNWDDVA VSLSADISRW HKVTESE
