O04348 (TPP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thylakoidal processing peptidase 1, chloroplastic
EC=3.4.21.89

Alternative name(s):
Signal peptidase I-1

Gene names

Name:	TPP1
Ordered Locus Names:	At2g30440
ORF Names:	T6B20.20

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Cleaves the thylakoid-transfer domain from a chloroplast protein. Ref.1
Catalytic activity	Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Subcellular location	Plastid › chloroplast thylakoid membrane; Single-pass membrane protein. Note: located in the non-appressed lamellae of the thylakoid network By similarity. Ref.1
Sequence similarities	Belongs to the peptidase S26 family.
Sequence caution	The sequence AAB63091.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Chloroplast Membrane Plastid Thylakoid
Domain	Transit peptide Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW signal peptide processing Inferred from direct assay Ref.1. Source: TAIR
Cellular component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	endopeptidase activity Inferred from direct assay Ref.1. Source: TAIR serine-type peptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 52	52	Chloroplast Potential
	Transit peptide	53 – ?		Thylakoid Potential
	Chain	? – 340		Thylakoidal processing peptidase 1, chloroplastic		PRO_0000310734
Regions
	Transmembrane	155 – 175	21	Helical; Potential
	Topological domain	176 – 340	165	Lumenal, thylakoid Potential
	Compositional bias	131 – 135	5	Poly-Asp
Sites
	Active site	184	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O04348 [UniParc]. Last modified November 1, 1998. Version 2. Checksum: F6763EBFC1DAA2E1	FASTA	340	37,853
	10 20 30 40 50 60 MAIRITFTYS THVARNLVGT RVGPGGYCFE SLVRPRFFSH KRDFDRSPRN RPASMYGSIA 70 80 90 100 110 120 RELIGEGSQS PLVMGLISIL KSTTGHESST MNVLGVSSFK ASSIIPFLQG SKWIKNPPVI 130 140 150 160 170 180 DDVDKGGTVC DDDDDKESRN GGSGWVNKLL SVCSEDAKAA FTAVTVSILF RSALAEPKSI 190 200 210 220 230 240 PSTSMYPTLD KGDRVMAEKV SYFFRKPEVS DIVIFKAPPI LLEYPEYGYS SNDVFIKRIV 250 260 270 280 290 300 ASEGDWVEVR DGKLFVNDIV QEEDFVLEPM SYEMEPMFVP KGYVFVLGDN RNKSFDSHNW 310 320 330 340 GPLPIENIVG RSVFRYWPPS KVSDTIYHDQ AITRGPVAVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana. Implications for the origin and catalytic mechanism of the enzyme." Chaal B.K., Mould R.M., Barbrook A.C., Gray J.C., Howe C.J. J. Biol. Chem. 273:689-692(1998) [PubMed: 9422718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Arabidopsis ORF clones." Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R. Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y10477 mRNA. Translation: CAA71502.1. U93215 Genomic DNA. Translation: AAB63091.1. Sequence problems. CP002685 Genomic DNA. Translation: AEC08389.1. AY128354 mRNA. Translation: AAM91557.1. BT020607 mRNA. Translation: AAW80880.1.
IPI	IPI00520820.
PIR	E84708.
RefSeq	NP_180603.2. NM_128597.2.
UniGene	At.10032.
3D structure databases
HSSP	HSSP built from PDB template 1KN9 based on UniProtKB P00803.
ProteinModelPortal	O04348.
SMR	O04348. Positions 171-321.
ModBase	Search...
Protein-protein interaction databases
STRING	O04348.
Protein family/group databases
MEROPS	S26.008.
Proteomic databases
PRIDE	O04348.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G30440.1; AT2G30440.1; AT2G30440.
GeneID	817595.
GenomeReviews	Gene locus AT2G30440 in contig CT485783_GR.
KEGG	ath:AT2G30440.
NMPDR	fig|3702.1.peg.10095.
Organism-specific databases
GeneFarm	2455. 205.
TAIR	At2g30440.
Phylogenomic databases
eggNOG	KOG0171.
GeneTree	EPGT00070000028654.
HOGENOM	HBG595105.
InParanoid	O04348.
OMA	MAIRITF.
PhylomeDB	O04348.
ProtClustDB	CLSN2682520.
Gene expression databases
Genevestigator	O04348.
Family and domain databases
InterPro	IPR000223. Pept_S26A_signal_pept_1. IPR019758. Pept_S26A_signal_pept_1_CS. IPR019756. Pept_S26A_signal_pept_1_Ser-AS. IPR015927. Peptidase_S24_S26A/B/C. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. IPR019533. Peptidase_S26. [Graphical view]
Gene3D	G3DSA:2.10.109.10. Pept_S24_S26_C. 2 hits.
KO	K03100.
Pfam	PF10502. Peptidase_S26. 1 hit. [Graphical view]
PRINTS	PR00727. LEADERPTASE.
SUPFAM	SSF51306. Pept_S24_S26_C. 1 hit.
TIGRFAMs	TIGR02227. Sigpep_I_bact. 1 hit.
PROSITE	PS00501. SPASE_I_1. 1 hit. PS00761. SPASE_I_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TPP1_ARATH

Accession

Primary (citable) accession number: O04348
Secondary accession number(s): Q7DM64

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	November 1, 1998
Last modified:	November 16, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program