Reviewed, UniProtKB/Swiss-Prot P42786 (PIP_NEIGO)

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

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes peptides having the structure Pro-Y-Z to yield free proline. Also hydrolyzes the dipeptide Pro-Gly.
Catalytic activity	Release of N-terminal proline from a peptide.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the peptidase S33 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	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 – 310	310	Proline iminopeptidase		PRO_0000080841
Sites
	Active site	107	1	Nucleophile By similarity
	Active site	260	1	By similarity
	Active site	287	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42786-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: D0E7AEBA908A1AE0	FASTA	310	34,792
	10 20 30 40 50 60 MYEIKQPFHS GYLQVSEIHQ IYWEESGNPD GVPVIFLHGG PGAGASPECR GFFNPDVFRI 70 80 90 100 110 120 VIIDQRGCGR SHPYACAEDN TTWDLVADIE KVREMLGIGK WLVFGGSWGS TLSLAYAQTH 130 140 150 160 170 180 PERVKGLVLR GIFLCRPSET AWLNEAGGVS RIYPEQWQKF VAPIAENRRN RLIEAYHGLL 190 200 210 220 230 240 FHQDEEVCLS AAKAWADWES YLIRFEPEGV DEDAYASLAI ARLENHYFVN GGWLQGDKAI 250 260 270 280 290 300 LNNIGKIRHI PTVIVQGRYD LCTPMQSAWE LSKAFPEAEL RVVQAGHCAF DPPLADALVQ 310 AVEDILPRLL

References

[1]	"Molecular cloning and characterization of a proline iminopeptidase gene from Neisseria gonorrhoeae." Albertson N.H., Koomey M. Mol. Microbiol. 9:1203-1211(1993) [PubMed: 7934933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10. Strain: MS11 / MSO1-1X.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z25461 Genomic DNA. Translation: CAA80948.1.
PIR	S39592.
3D structure databases
HSSP	HSSP built from PDB template 1AZW based on UniProtKB P52279.
ModBase	Search...
Protein family/group databases
MEROPS	S33.001.
Enzyme and pathway databases
BRENDA	3.4.11.5. 588.
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.
ProDom	PD001189. Peptidase_S10. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01249. pro_imino_pep_1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PIP_NEIGO

Accession

Primary (citable) accession number: P42786

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 65 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)