Reviewed, UniProtKB/Swiss-Prot P52279 (PIP_XANCI)

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
Synonyms:	xap

Organism

Xanthomonas campestris pv. citri

Taxonomic identifier

346 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May be involved in proline metabolism and sensitivity to ascamycin. Has ascamycin dealanylating activity.
Catalytic activity	Release of N-terminal proline from a peptide.
Subunit structure	Homooligomer.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase S33 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
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 – 313

313

Proline iminopeptidase

PRO_0000080847

Sites

Active site

110

1

Nucleophile Ref.4

Active site

266

1

Ref.4

Active site

294

1

Proton donor Ref.4

Experimental info

Sequence conflict

95

1

L → V in BAA11623. Ref.3

Sequence conflict

121 – 129

9

ADPSAAGHQ → QTHPQQVTE in BAA11623. Ref.3

Sequence conflict

245 – 251

7

QLLRDAH → SCCATD in BAA11623. Ref.3

Sequence conflict

284

1

Missing in BAA11623. Ref.3

Secondary structure

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313

Helix Strand Turn

Details...

Beta strand

11 – 17

7

Beta strand

19 – 21

3

Beta strand

23 – 30

8

Beta strand

34 – 40

7

Turn

43 – 46

4

Helix

50 – 55

6

Turn

58 – 60

3

Beta strand

61 – 66

6

Beta strand

74 – 76

3

Helix

85 – 98

14

Beta strand

102 – 109

8

Helix

111 – 122

12

Helix

124 – 126

3

Beta strand

127 – 134

8

Helix

140 – 147

8

Helix

151 – 154

4

Helix

156 – 164

9

Helix

168 – 170

3

Helix

174 – 182

9

Helix

187 – 203

17

Beta strand

205 – 208

4

Helix

211 – 217

7

Helix

220 – 235

16

Helix

237 – 239

3

Helix

245 – 248

4

Helix

250 – 253

4

Beta strand

258 – 263

6

Beta strand

267 – 269

3

Helix

271 – 280

10

Beta strand

284 – 289

6

Helix

299 – 312

14

Sequences

	Sequence		Length	Mass (Da)
	P52279-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 7A9DF2636363FF48	FASTA	313	35,260
	10 20 30 40 50 60 MRTLYPEITP YQQGSLKVDD RHTLYFEQCG NPHGKPVVML HGGPGGGCND KMRRFHDPAK 70 80 90 100 110 120 YRIVLFDQRG SGRSTPHADL VDNTTWDLVA DIERLRTHLG VDRWQVFGGS WGSTLALAYA 130 140 150 160 170 180 ADPSAAGHQL VLRGIFLLRR FELEWFYQEG ASRLFPDAWE HYLNAIPPVE RADLMSAFHR 190 200 210 220 230 240 RLTSDDEATR LAAAKAWSVW EGATSFLHVD EDFVTGHEDA HFALAFARIE NHYFVNGGFF 250 260 270 280 290 300 EVEDQLLRDA HRIADIPGVI VHGRYDVVCP LQSAWDLHKA WPKAQLQISP ASGHSAFEPE 310 NVDALVRATD GFA

References

[1]	"Proline iminopeptidase gene from Xanthomonas campestris pv. citri." Alonso J., Garcia J.L. Microbiology 142:2951-2957(1996) [PubMed: 8885412] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IFO 3835.
[2]	Alonso J. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Isolation and characterization of the gene encoding an aminopeptidase involved in the selective toxicity of ascamycin toward Xanthomonas campestris pv. citri." Sudo T., Shinohara K., Dohmae N., Takio K., Usami R., Horikoshi K., Osada H. Biochem. J. 319:99-102(1996) [PubMed: 8870654] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20 AND 283-296. Strain: IFO 3781.
[4]	"Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family." Medrano F.J., Alonso J., Garcia J.L., Romero A., Bode W., Gomis-Ruth F.X. EMBO J. 17:1-9(1998) [PubMed: 9427736] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z54150 Genomic DNA. Translation: CAA90864.1.
D82882 Genomic DNA. Translation: BAA11623.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AZW	X-ray	2.70	A/B	1-313	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S33.001.

Family and domain databases

InterPro

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

Pfam

PF00561. Abhydrolase_1. 1 hit.
[Graphical view]

PIRSF

PIRSF006431. Pept_S33. 1 hit.

PRINTS

PR00793. PROAMNOPTASE.

TIGRFAMs

TIGR01249. pro_imino_pep_1. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PIP_XANCI

Accession

Primary (citable) accession number: P52279
Secondary accession number(s): P96186

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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