Reviewed, UniProtKB/Swiss-Prot O83142 (5NTD_TREPA)

Names and origin

Protein names

Recommended name:
    Probable 5'-nucleotidase
    EC=3.1.3.5

Gene names

Ordered Locus Names:

TP_0104

Organism

Treponema pallidum [Complete proteome] [HAMAP]

Taxonomic identifier

160 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Treponema

Protein attributes

Sequence length	593 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Cofactor	Divalent cations By similarity.
Subcellular location	Cell membrane; Lipid-anchor Potential.
Sequence similarities	Belongs to the 5'-nucleotidase family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Lipoprotein Palmitate
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nucleotide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	5'-nucleotidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 593	572	Probable 5'-nucleotidase		PRO_0000000027
Regions
	Region	539 – 545	7	Substrate binding By similarity
Sites
	Metal binding	41	1	Divalent metal cation 1 By similarity
	Metal binding	43	1	Divalent metal cation 1 By similarity
	Metal binding	91	1	Divalent metal cation 1 By similarity
	Metal binding	91	1	Divalent metal cation 2 By similarity
	Metal binding	123	1	Divalent metal cation 2 By similarity
	Metal binding	224	1	Divalent metal cation 2 By similarity
	Binding site	456	1	Substrate By similarity
	Site	124	1	Transition state stabilizer By similarity
	Site	127	1	Transition state stabilizer By similarity
Amino acid modifications
	Lipidation	22	1	N-palmitoyl cysteine Probable
	Lipidation	22	1	S-diacylglycerol cysteine Probable

Sequences

	Sequence		Length	Mass (Da)
	O83142-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 051931037DF33B40	FASTA	593	64,871
	10 20 30 40 50 60 MKRFIPHRVI HAVCIGLALV GCRKLDSRAG DFELTIIHIN DHHSHLEPEP LELAVAGERL 70 80 90 100 110 120 RAAVGGYAAL VHEIQRLRAE SKNALVLHAG DALIGTLYST LFRGRADAVL MNHAGFDFFT 130 140 150 160 170 180 LGNHEFDNGN EGLKEFLHYL EVPVLSANVV PNAASTLHGL WKPSAIVERA GERIGVIGLD 190 200 210 220 230 240 TVKKTVESSS PGKDINFIDE IEAVRRATVE MQQQGVNKII LLSHAGFEKN CEIAQNISGI 250 260 270 280 290 300 DVIVSGDTHY LLGDESLGRL GLPVVGEYPR KIMSPAGEPV YVVEAWEYGK CLGELNVVFD 310 320 330 340 350 360 RTGVITSAVG MPRFLLHTNT LQKKGADRKN YPLEEAEREA LLVALRMTPE IIFAQENDQI 370 380 390 400 410 420 ISVLEEFKKE KEALGAQAIG VITGASMRGG SVHRVPDAQN PQGSVATRFV AETMLSDIQS 430 440 450 460 470 480 FGAGKVDCVI QNAGGARSNI QPGEITYNDA YTLLPFSNTL VLVDVSGAEL KQIIEDALQF 490 500 510 520 530 540 ALGDGSTGAF PYGAGVRYEA RQEPDEHGKR VIKLEVQKKD GAWVPVDERA PYRLGVNSYI 550 560 570 580 590 ARGKDGYKTL GEIVSTRGAE DTYLRDAESL IKFLRAHKNF RAYTDSNVIF RLK

References

[1]

"Complete genome sequence of Treponema pallidum, the syphilis spirochete." Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., Khalak H.G., Richardson D.L., Howell J.K. , Chidambaram M., Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O., Venter J.C. Science 281:375-388(1998) [PubMed: 9665876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nichols.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000520 Genomic DNA. Translation: AAC26552.1.
PIR	E71365.
RefSeq	NP_218544.1.
3D structure databases
HSSP	HSSP built from PDB template 2USH based on UniProtKB P07024.
ModBase	Search...
Protein-protein interaction databases
IntAct	O83142. 11 interactions.
Genome annotation databases
GeneID	2610818.
GenomeReviews	Gene locus TP_0104 in contig AE000520_GR.
KEGG	tpa:TP0104.
NMPDR	fig|243276.1.peg.103.
TIGR	TP_0104.
Phylogenomic databases
HOGENOM	O83142.
OMA	RIATRAQ.
Enzyme and pathway databases
BioCyc	TPAL243276:TP_0104-MON.
BRENDA	3.1.3.5. 142600.
Family and domain databases
InterPro	IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR004843. M-pesterase. IPR006420. NadN. [Graphical view]
Gene3D	G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit.
PANTHER	PTHR11575. 5_nucleotidase. 1 hit.
Pfam	PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR01607. APYRASEFAMLY.
TIGRFAMs	TIGR01530. nadN. 1 hit.
PROSITE	PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. PS51257. PROKAR_LIPOPROTEIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

5NTD_TREPA

Accession

Primary (citable) accession number: O83142

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1998
Last modified:	November 3, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)