5NTD_TREPA
ID 5NTD_TREPA Reviewed; 593 AA.
AC O83142;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable 5'-nucleotidase;
DE EC=3.1.3.5;
DE Flags: Precursor;
GN OrderedLocusNames=TP_0104;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; AE000520; AAC26552.1; -; Genomic_DNA.
DR PIR; E71365; E71365.
DR RefSeq; WP_010881553.1; NC_021490.2.
DR AlphaFoldDB; O83142; -.
DR SMR; O83142; -.
DR IntAct; O83142; 11.
DR STRING; 243276.TPANIC_0104; -.
DR EnsemblBacteria; AAC26552; AAC26552; TP_0104.
DR GeneID; 57878644; -.
DR KEGG; tpa:TP_0104; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_7_1_12; -.
DR OMA; VQPFTNM; -.
DR OrthoDB; 1884225at2; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
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 InterPro; IPR006420; NadN.
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 TIGRFAMs; TIGR01530; nadN; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Nucleotide-binding; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..593
FT /note="Probable 5'-nucleotidase"
FT /id="PRO_0000000027"
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 91
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 539..545
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 124
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 64871 MW; 051931037DF33B40 CRC64;
MKRFIPHRVI HAVCIGLALV GCRKLDSRAG DFELTIIHIN DHHSHLEPEP LELAVAGERL
RAAVGGYAAL VHEIQRLRAE SKNALVLHAG DALIGTLYST LFRGRADAVL MNHAGFDFFT
LGNHEFDNGN EGLKEFLHYL EVPVLSANVV PNAASTLHGL WKPSAIVERA GERIGVIGLD
TVKKTVESSS PGKDINFIDE IEAVRRATVE MQQQGVNKII LLSHAGFEKN CEIAQNISGI
DVIVSGDTHY LLGDESLGRL GLPVVGEYPR KIMSPAGEPV YVVEAWEYGK CLGELNVVFD
RTGVITSAVG MPRFLLHTNT LQKKGADRKN YPLEEAEREA LLVALRMTPE IIFAQENDQI
ISVLEEFKKE KEALGAQAIG VITGASMRGG SVHRVPDAQN PQGSVATRFV AETMLSDIQS
FGAGKVDCVI QNAGGARSNI QPGEITYNDA YTLLPFSNTL VLVDVSGAEL KQIIEDALQF
ALGDGSTGAF PYGAGVRYEA RQEPDEHGKR VIKLEVQKKD GAWVPVDERA PYRLGVNSYI
ARGKDGYKTL GEIVSTRGAE DTYLRDAESL IKFLRAHKNF RAYTDSNVIF RLK
