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Protein

Preflagellin peptidase

Gene

flaK

Organism
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the N-terminal leader peptide from preflagellins.1 Publication

Catalytic activityi

Cleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly-|- or Lys-Gly-|-, to release flagellin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei18 – 181Essential for catalysisBy similarity
Sitei79 – 791Essential for catalysisBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Keywords - Biological processi

Archaeal flagellum biogenesis

Enzyme and pathway databases

BioCyciMMAR444158:GHN2-339-MONOMER.
BRENDAi3.4.23.52. 3262.

Protein family/group databases

MEROPSiA24.016.

Names & Taxonomyi

Protein namesi
Recommended name:
Preflagellin peptidase (EC:3.4.23.52)
Short name:
PFP
Gene namesi
Name:flaK
Ordered Locus Names:MmarC6_0338
OrganismiMethanococcus maripaludis (strain C6 / ATCC BAA-1332)
Taxonomic identifieri444158 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000000791 Componenti: Chromosome

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 11CytoplasmicCurated
Transmembranei2 – 1817HelicalCuratedAdd
BLAST
Topological domaini19 – 235ExtracellularCurated
Transmembranei24 – 4623HelicalCuratedAdd
BLAST
Topological domaini47 – 493CytoplasmicCurated
Transmembranei50 – 7223HelicalCuratedAdd
BLAST
Topological domaini73 – 786ExtracellularCurated
Transmembranei79 – 8911HelicalCuratedAdd
BLAST
Topological domaini90 – 11021CytoplasmicCuratedAdd
BLAST
Transmembranei111 – 13929HelicalCuratedAdd
BLAST
Topological domaini140 – 20465ExtracellularCuratedAdd
BLAST
Transmembranei205 – 21612HelicalCuratedAdd
BLAST
Topological domaini217 – 23014CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231E → A: No effect on proteolytic activity. 1 Publication
Mutagenesisi25 – 251E → A: No effect on proteolytic activity. 1 Publication
Mutagenesisi26 – 261D → A: No effect on proteolytic activity. 1 Publication
Mutagenesisi76 – 761G → A: Large reduction in proteolytic activity. 1 Publication
Mutagenesisi77 – 771G → A: No effect on proteolytic activity. 1 Publication
Mutagenesisi78 – 781G → A: No effect on proteolytic activity. 1 Publication
Mutagenesisi208 – 2081P → A: Enhanced proteolytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230230Preflagellin peptidasePRO_0000419277Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi444158.MmarC6_0338.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S0XX-ray3.60A/B1-230[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG02298. Archaea.
COG1989. LUCA.
HOGENOMiHOG000254257.
KOiK07991.
OMAiEIEDYIW.

Family and domain databases

InterProiIPR009655. Preflagellin_peptidase_C.
IPR000045. Prepilin_IV_endopep_pep.
[Graphical view]
PfamiPF06847. Arc_PepC_II. 1 hit.
PF01478. Peptidase_A24. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9A677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEYIIGALG LIIASVQDFR SREIEDYIWI FLAVFGVLFA IYSSITLLDY
60 70 80 90 100
SILINSISGF VICFILGYMM FLSGIGGGDG KMLIGLGALV PKFQMPIYTS
110 120 130 140 150
LGTLLNLNYV PTFPIMVFIN GIFFMVFLPF VILFRNILNG ARPKTGKEFI
160 170 180 190 200
LMFFGEKMKV NVAKEQKRLI MGQNDKINFF PAADDEDFSK YSNNEEIWVT
210 220 230
PQIPLIIPIT LSYLVTPIIG DRILDFLIPF
Length:230
Mass (Da):26,021
Last modified:January 15, 2008 - v1
Checksum:i879C0EE8E214E61A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000867 Genomic DNA. Translation: ABX01159.1.
RefSeqiWP_012193134.1. NC_009975.1.

Genome annotation databases

EnsemblBacteriaiABX01159; ABX01159; MmarC6_0338.
GeneIDi5739084.
KEGGimmx:MmarC6_0338.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000867 Genomic DNA. Translation: ABX01159.1.
RefSeqiWP_012193134.1. NC_009975.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S0XX-ray3.60A/B1-230[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi444158.MmarC6_0338.

Protein family/group databases

MEROPSiA24.016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX01159; ABX01159; MmarC6_0338.
GeneIDi5739084.
KEGGimmx:MmarC6_0338.

Phylogenomic databases

eggNOGiarCOG02298. Archaea.
COG1989. LUCA.
HOGENOMiHOG000254257.
KOiK07991.
OMAiEIEDYIW.

Enzyme and pathway databases

BioCyciMMAR444158:GHN2-339-MONOMER.
BRENDAi3.4.23.52. 3262.

Family and domain databases

InterProiIPR009655. Preflagellin_peptidase_C.
IPR000045. Prepilin_IV_endopep_pep.
[Graphical view]
PfamiPF06847. Arc_PepC_II. 1 hit.
PF01478. Peptidase_A24. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C6 / ATCC BAA-1332.
  2. "The crystal structure of GXGD membrane protease FlaK."
    Hu J., Xue Y., Lee S., Ha Y.
    Nature 475:528-531(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-23; GLU-25; ASP-26; GLY-76; GLY-77; GLY-78 AND PRO-208.
    Strain: C6 / ATCC BAA-1332.

Entry informationi

Entry nameiFLAK_METM6
AccessioniPrimary (citable) accession number: A9A677
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: January 15, 2008
Last modified: November 11, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.