O32449 (PIP_SERMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proline iminopeptidase
Short name=PIP
EC=3.4.11.5

Alternative name(s):
Prolyl aminopeptidase
Short name=PAP

Gene names

Name:

pip

Organism

Serratia marcescens

Taxonomic identifier

615 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specifically catalyzes the removal of N-terminal proline residues from peptides.
Catalytic activity	Release of N-terminal proline from a peptide.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the peptidase S33 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	3D-structure
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase activity 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

Chain

1 – 317

317

Proline iminopeptidase

PRO_0000080845

Sites

Active site

113

1

Nucleophile

Active site

268

1

Active site

296

1

Proton donor

Secondary structure

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317

Helix Strand Turn

Details...

Beta strand

14 – 20

7

Beta strand

22 – 24

3

Beta strand

26 – 33

8

Beta strand

37 – 43

7

Turn

46 – 48

3

Helix

53 – 56

4

Turn

61 – 63

3

Beta strand

64 – 69

6

Beta strand

72 – 74

3

Helix

88 – 102

15

Beta strand

105 – 112

8

Helix

114 – 123

10

Beta strand

129 – 137

9

Helix

143 – 150

8

Beta strand

152 – 154

3

Helix

155 – 157

3

Helix

159 – 167

9

Helix

172 – 176

5

Helix

177 – 185

9

Helix

190 – 207

18

Beta strand

208 – 211

4

Helix

214 – 219

6

Helix

222 – 237

16

Helix

239 – 241

3

Turn

245 – 251

7

Helix

252 – 255

4

Beta strand

260 – 265

6

Beta strand

269 – 271

3

Helix

273 – 282

10

Beta strand

286 – 291

6

Helix

301 – 315

15

Sequences

	Sequence		Length	Mass (Da)
	O32449 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 48A427C9B97D972D	FASTA	317	36,084
	10 20 30 40 50 60 MEQLRGLYPP LAAYDSGWLD TGDGHRIYWE LSGNPNGKPA VFIHGGPGGG ISPHHRQLFD 70 80 90 100 110 120 PERYKVLLFD QRGCGRSRPH ASLDNNTTWH LVADIERLRE MAGVEQWLVF GGSWGSTLAL 130 140 150 160 170 180 AYAQTHPERV SEMVLRGIFT LRKQRLHWYY QDGASRFFPE KWERVLSILS DDERKDVIAA 190 200 210 220 230 240 YRQRLTSADP QVQLEAAKLW SVWEGETVTL LPSRESASFG EDDFALAFAR IENHYFTHLG 250 260 270 280 290 300 FLESDDQLLR NVPLIRHIPA VIVHGRYDMA CQVQNAWDLA KAWPEAELHI VEGAGHSYDE 310 PGILHQLMIA TDRFAGK

References

[1]	"Prolyl aminopeptidase from Serratia marcescens: cloning of the enzyme gene and crystallization of the expressed enzyme." Kabashima T., Kitazono A., Kitano A., Ito K., Yoshimoto T. J. Biochem. 122:601-605(1997) [PubMed: 9348090] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Substrate recognition mechanism of prolyl aminopeptidase from Serratia marcescens." Ito K., Inoue T., Kabashima T., Kanada N., Huang H.S., Ma X., Azmi N., Azab E., Yoshimoto T. J. Biochem. 128:673-678(2000) [PubMed: 11011150] [Abstract] Cited for: MUTAGENESIS.
[3]	"Crystal structure of prolyl aminopeptidase from Serratia marcescens." Yoshimoto T., Kabashima T., Uchikawa K., Inoue T., Tanaka N., Nakamura K.T., Tsuru M., Ito K. J. Biochem. 126:559-565(1999) [PubMed: 10467172] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D87897 Genomic DNA. Translation: BAA23336.1.

PIR

JC5696.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QTR	X-ray	2.32	A	1-317	[»]
1WM1	X-ray	2.10	A	1-317	[»]
1X2B	X-ray	2.40	A	1-317	[»]
1X2E	X-ray	2.40	A	1-317	[»]

ProteinModelPortal

O32449.

SMR

O32449. Positions 4-317.

ModBase

Search...

Protein family/group databases

MEROPS

S33.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000073. AB_hydrolase_1.
IPR005944. Pept_S33.
IPR002410. Peptidase_S33.
[Graphical view]

PANTHER

PTHR10992:SF12. PTHR10992:SF12. 1 hit.

Pfam

PF00561. Abhydrolase_1. 1 hit.
[Graphical view]

PIRSF

PIRSF006431. Pept_S33. 1 hit.

PRINTS

PR00111. ABHYDROLASE.
PR00793. PROAMNOPTASE.

TIGRFAMs

TIGR01249. Pro_imino_pep_1. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PIP_SERMA

Accession

Primary (citable) accession number: O32449

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 1, 1998
Last modified:	November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program