Hydrogenase 3 maturation protease - Escherichia coli (strain K12)

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P0AEV9 (HYCI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Hydrogenase 3 maturation protease
EC=3.4.23.51

Alternative name(s):
HycI protease

Gene names

Name:	hycI
Ordered Locus Names:	b2717, JW2687

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protease involved in the C-terminal processing of hycE, the large subunit of hydrogenase 3.
Catalytic activity	This enzyme specifically removes a 32-amino acid peptide from the C-terminus of the precursor of the large subunit of E.coli hydrogenase 3 by cleavage at the C-terminal side of Arg(537).
Subunit structure	Monomer.
Sequence similarities	Belongs to the peptidase A31 family.

Ontologies

Keywords
Ligand	Metal-binding Nickel
Molecular function	Aspartyl protease Hydrolase Protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW enzyme activator activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
aceE	P0AFG8	1	EBI-552628,EBI-542683

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1

Chain

2 – 156

155

Hydrogenase 3 maturation protease

PRO_0000201944

Sites

Metal binding

Nickel By similarity

Metal binding

Nickel By similarity

Metal binding

Nickel By similarity

Experimental info

Mutagenesis

D → N: No protease activity. Ref.4

Mutagenesis

D → N or M: No protease activity. Ref.4

Mutagenesis

H → Q: A little protease activity remaining. Ref.4

Secondary structure

156

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEV9 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CCE90535AFC0F30D
Show »

FASTA

156

17,057

        10         20         30         40         50         60 
MTDVLLCVGN SMMGDDGAGP LLAEKCAAAP KGNWVVIDGG SAPENDIVAI RELRPTRLLI 

        70         80         90        100        110        120 
VDATDMGLNP GEIRIIDPDD IAEMFMMTTH NMPLNYLIDQ LKEDIGEVIF LGIQPDIVGF 

       130        140        150 
YYPMTQPIKD AVETVYQRLE GWEGNGGFAQ LAVEEE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterisation of a protease from Escherichia coli involved in hydrogenase maturation." Rossmann R., Maier T., Lottspeich F., Boeck A. Eur. J. Biochem. 227:545-550(1995) [PubMed: 7851435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-37 AND 66-84. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation." Theodoratou E., Paschos A., Magalon A., Fritsche E., Huber R., Boeck A. Eur. J. Biochem. 267:1995-1999(2000) [PubMed: 10727938] [Abstract] Cited for: MUTAGENESIS OF ASP-16; ASP-62 AND HIS-90, INVOLVEMENT OF NICKEL ION BINDING IN PROTEASE ACTIVITY. Strain: K12 / JM109 / ATCC 53323.
[5]	"Solution structure and backbone dynamics of an endopeptidase HycI from Escherichia coli: implications for mechanism of the [NiFe] hydrogenase maturation." Yang F., Hu W., Xu H., Li C., Xia B., Jin C. J. Biol. Chem. 282:3856-3863(2007) [PubMed: 17150961] [Abstract] Cited for: STRUCTURE BY NMR.
[6]	"Crystal structure of hydrogenase maturating endopeptidase HycI from Escherichia coli." Kumarevel T., Tanaka T., Bessho Y., Shinkai A., Yokoyama S. Biochem. Biophys. Res. Commun. 389:310-314(2009) [PubMed: 19720045] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-156 IN COMPLEX WITH CALCIUM IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X17506 Genomic DNA. Translation: CAA35554.1.
U29579 Genomic DNA. Translation: AAA69227.1.
U00096 Genomic DNA. Translation: AAC75759.1.
AP009048 Genomic DNA. Translation: BAE76794.1.

PIR

S67469.

RefSeq

NP_417197.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E85	X-ray	1.70	A/B	2-156	[»]
2I8L	NMR	-	A	1-156	[»]

ProteinModelPortal

P0AEV9.

SMR

P0AEV9. Positions 1-156.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48019N.

IntAct

P0AEV9. 9 interactions.

MINT

MINT-1244231.

Protein family/group databases

MEROPS

A31.003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004414; EBESCP00000004414; EBESCG00000003601.
EBESCT00000018342; EBESCP00000017633; EBESCG00000017396.

GeneID

947428.

GenomeReviews

Gene locus JW2687 in contig AP009048_GR.
Gene locus b2717 in contig U00096_GR.

KEGG

ecj:JW2687.
eco:b2717.

PATRIC

32120834. VBIEscCol129921_2809.

Organism-specific databases

EchoBASE

EB3177.

EcoGene

EG13396. hycI.

Phylogenomic databases

eggNOG

COG0680.

GeneTree

EBGT00050000009077.

HOGENOM

HBG730254.

OMA

MPLNYLV.

PhylomeDB

P0AEV9.

ProtClustDB

PRK11544.

Enzyme and pathway databases

BioCyc

EcoCyc:G7414-MONOMER.
MetaCyc:G7414-MONOMER.

Gene expression databases

Genevestigator

P0AEV9.

Family and domain databases

InterPro

IPR004420. Pept_A31_hyd_mat_HycI.
IPR023430. Pept_HybD-like_dom.
IPR000671. Peptidase_A31.
[Graphical view]

Gene3D

G3DSA:3.40.50.1450. Peptidase_A31. 1 hit.

K08315.

Pfam

PF01750. HycI. 1 hit.
[Graphical view]

PRINTS

PR00446. HYDRGNUPTAKE.

SUPFAM

SSF53163. SSF53163. 1 hit.

TIGRFAMs

TIGR00142. HycI. 1 hit.
TIGR00072. Hydrog_prot. 1 hit.

ProtoNet

Search...

Entry information

Entry name

HYCI_ECOLI

Accession

Primary (citable) accession number: P0AEV9
Secondary accession number(s): Q2MAB2, Q57451

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents