ID G5R8F1_SALSE Unreviewed; 518 AA.
AC G5R8F1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=5'-nucleotidase {ECO:0000313|EMBL:EHC79561.1};
GN ORFNames=LTSESEN_6068 {ECO:0000313|EMBL:EHC79561.1};
OS Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC79561.1, ECO:0000313|Proteomes:UP000005065};
RN [1] {ECO:0000313|EMBL:EHC79561.1, ECO:0000313|Proteomes:UP000005065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-543 {ECO:0000313|EMBL:EHC79561.1,
RC ECO:0000313|Proteomes:UP000005065};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|ARBA:ARBA00006654, ECO:0000256|RuleBase:RU362119}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC79561.1}.
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DR EMBL; AFCU01001918; EHC79561.1; -; Genomic_DNA.
DR AlphaFoldDB; G5R8F1; -.
DR PATRIC; fig|913082.3.peg.4759; -.
DR BioCyc; SENT913082:G120J-638-MONOMER; -.
DR Proteomes; UP000005065; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd00845; MPP_UshA_N_like; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 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; 5'-NUCLEOTIDASE-RELATED; 1.
DR PANTHER; PTHR11575:SF46; PROTEIN USHA; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362119}; Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 21..518
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5005132477"
FT DOMAIN 24..252
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 330..476
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 518 AA; 56553 MW; A5DE4DCE9BBC0602 CRC64;
MKVKLLAAGI LFTLPFWACA KDVTIIYTND LHAHVEPYKV PWIADGKRDI GGWANITTLV
KQEKAKNKAT WFFDAGDYFT GPYISSLTKG KAIIDILNTM QYDAATIGNH EFDHGWDNTL
LQLSRAKFPI VQGNIFYEDS SKSFWDKPYT IVEKDGVKIG VIGLHGVFAF NDTVSAATRV
GIEARDEIKW LQRYIDELKG KVDLTVALIH EGTPARQSSM GNTDVRRALD KDIQTASQVK
GLDILITGHA HVGTPEPIKV GNTLILSTDS GGIDVGKLVL DYQEKPHQFT VKNFELKTIF
ADEWKPDPQT KQVIDGWNKK LDKVVQQTVA QSPVELTRAY GESSSLGNLA ADALLFTAGK
DTQLALTNSG GIRNEIPAGA VTMGAVISTF PFPNELVTMD LTGKQLRSLM EHGAGLSNGV
LQVSKGLEMK YDSSKPVGQR VTVLTLNGKP IDDATVYHIA TNSFLADGGD GFAAFTEGQA
RNTSGGYYVS NAIVDYFKAG NTITDEQLKG MRVADVKK
//