USHA_SALTY
ID USHA_SALTY Reviewed; 550 AA.
AC P06196; Q9R369; Q9RN34; Q9RN35; Q9RN36;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Silent protein UshA(0);
DE Flags: Precursor;
GN Name=ushA; OrderedLocusNames=STM0494;
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].
RX PubMed=3031310; DOI=10.1016/0022-2836(86)90358-x;
RA Burns D.M., Beacham I.R.;
RT "Identification and sequence analysis of a silent gene (ushA0) in
RT Salmonella typhimurium.";
RL J. Mol. Biol. 192:163-175(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CDC 1119-83, CDC 137-85, CDC 179-87, CDC 331-86, and CDC 655-84;
RX PubMed=11429465; DOI=10.1099/00221287-147-7-1887;
RA Innes D., Beacham I.R., Beven C.-A., Douglas M., Laird M.W., Joly J.C.,
RA Burns D.M.;
RT "The cryptic ushA gene (ushA(c)) in natural isolates of Salmonella enterica
RT (serotype Typhimurium) has been inactivated by a single missense
RT mutation.";
RL Microbiology 147:1887-1896(2001).
RN [3]
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).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; X04651; CAA28348.1; -; Genomic_DNA.
DR EMBL; AF188728; AAF05582.1; -; Genomic_DNA.
DR EMBL; AF188729; AAF05583.1; -; Genomic_DNA.
DR EMBL; AF188730; AAF05584.1; -; Genomic_DNA.
DR EMBL; AF188731; AAF05585.1; -; Genomic_DNA.
DR EMBL; AF188732; AAF05586.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19448.1; -; Genomic_DNA.
DR PIR; A26076; A26076.
DR RefSeq; NP_459489.1; NC_003197.2.
DR RefSeq; WP_000670407.1; NC_003197.2.
DR AlphaFoldDB; P06196; -.
DR SMR; P06196; -.
DR STRING; 99287.STM0494; -.
DR PaxDb; P06196; -.
DR EnsemblBacteria; AAL19448; AAL19448; STM0494.
DR GeneID; 1252014; -.
DR KEGG; stm:STM0494; -.
DR PATRIC; fig|99287.12.peg.528; -.
DR HOGENOM; CLU_005854_7_0_6; -.
DR PhylomeDB; P06196; -.
DR BioCyc; SENT99287:STM0494-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IBA:GO_Central.
DR GO; GO:0009166; P:nucleotide catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Metal-binding; Nucleotide-binding; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..550
FT /note="Silent protein UshA(0)"
FT /id="PRO_0000000033"
FT BINDING 41
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 498..504
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 117
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 258..275
FT /evidence="ECO:0000250"
FT VARIANT 139
FT /note="Y -> S (in strain: CDC 137-85 and CDC 179-87)"
FT VARIANT 197
FT /note="K -> N (in strain: CDC 137-85)"
FT VARIANT 388
FT /note="V -> G (in strain: CDC 179-87)"
FT VARIANT 393
FT /note="Q -> H (in strain: CDC 179-87)"
FT VARIANT 414
FT /note="E -> D (in strain: CDC 179-87)"
FT VARIANT 449
FT /note="A -> R (in strain: CDC 179-87, CDC 331-86 and CDC
FT 655-84)"
FT VARIANT 463
FT /note="L -> F (in strain: CDC 137-85)"
FT VARIANT 538
FT /note="A -> T (in strain: CDC 137-85)"
FT VARIANT 544
FT /note="N -> K (in strain: CDC 137-85)"
FT CONFLICT 396
FT /note="R -> G (in Ref. 1; CAA28348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 60557 MW; C4A798B75135F059 CRC64;
MKFLKRGVAL ALLAAFALTT QPAQAYEKDK TYKITILHTN DHHGHFWRSE YGEYGLAAQK
TLVDSIRKEV AQEGGSVLLL SGGDINTGVP ESDLQDAEPD FRGMNLIGYD AMAVGNHEFD
NPLTVLRQQE KWAKFPFLYA NIYQKSTGER LFKPWAIFTR QDIKIAVIGL TTDDTAKIGN
PEYFTDIEFR KPAEEAKVVI QELNMNEKPD VIIATTHMGH YDNGDHGSNA PGDVEMARSL
PAGSLAMIVG GHSQDPVCMA SENKKQVNYV PGTPCAPDKQ NGIWIVQAHE WGKYVGRADF
EFRNGEMKMV NYQLIPVNLK KKVTWDNGKS ERVLYTPEIA ENPQMLSLLT PFQNKGKAQL
EVKIGSVNGL LEGDRSKVRF VQTNMGRVIL AAQIARTGAD FGVMSGGGIR DSIEAGDITY
KSVLKVQPFG NIVVYADMSG KEVVDYLTAV AQMKPDSGAY PQLANVSFVA KEGKLTDLKI
KGEPVDPAKT YRMATLSFNA TGGDGYPRID NKPGYVNTGF IDAEVLKEFI QQNSPLDAAA
FTPNGEVSWL
