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Protein

Archaeal Lon protease

Gene

AF_0364

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei509 – 5091
Active sitei509 – 5091PROSITE-ProRule annotation
Active sitei552 – 5521
Active sitei552 – 5521PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi54 – 618ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-374-MONOMER.
BRENDAi3.4.21.53. 414.

Protein family/group databases

MEROPSiS16.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Archaeal Lon protease (EC:3.4.21.-)
Alternative name(s):
ATP-dependent protease La homolog
Gene namesi
Ordered Locus Names:AF_0364
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 117117CytoplasmicSequence analysisAdd
BLAST
Transmembranei118 – 13619HelicalSequence analysisAdd
BLAST
Topological domaini137 – 1415ExtracellularSequence analysis
Transmembranei142 – 16019HelicalSequence analysisAdd
BLAST
Topological domaini161 – 621461CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi506 – 5061E → A: Slightly decreases proteolytic activity.
Mutagenesisi508 – 5081D → A: No effect.
Mutagenesisi509 – 5091S → A: Completely abolishes proteolytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 621621Archaeal Lon proteasePRO_0000076151Add
BLAST

Interactioni

Subunit structurei

Homohexamer. Organized in a ring with a central cavity (By similarity).By similarity

Protein-protein interaction databases

STRINGi224325.AF0364.

Structurei

Secondary structure

1
621
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi422 – 4254Combined sources
Beta strandi428 – 4358Combined sources
Turni436 – 4383Combined sources
Beta strandi439 – 45113Combined sources
Helixi467 – 48519Combined sources
Helixi489 – 4913Combined sources
Beta strandi492 – 5009Combined sources
Beta strandi503 – 5064Combined sources
Helixi512 – 52312Combined sources
Beta strandi531 – 5333Combined sources
Beta strandi541 – 5444Combined sources
Helixi549 – 55810Combined sources
Beta strandi562 – 5676Combined sources
Helixi568 – 5736Combined sources
Turni578 – 5825Combined sources
Beta strandi583 – 5919Combined sources
Helixi592 – 5998Combined sources
Helixi604 – 62017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z0BX-ray1.55A415-621[»]
1Z0CX-ray1.55A415-621[»]
1Z0EX-ray2.05A/B/C/D/E/F417-621[»]
1Z0GX-ray2.27A/B/C/D/E/F417-621[»]
1Z0TX-ray3.00A/B/C/D/E/F417-621[»]
1Z0VX-ray3.00A/B/C/D/E/F417-621[»]
1Z0WX-ray1.20A415-621[»]
ProteinModelPortaliO29883.
SMRiO29883. Positions 416-621.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO29883.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini423 – 602180Lon proteolyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Lon proteolytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG02160. Archaea.
COG1067. LUCA.
KOiK04076.
OMAiDVHIQFV.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR004663. Lon_arc.
IPR027065. Lon_Prtase.
IPR000523. Mg_chelatse_chII_dom.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR002078. Sigma_54_int.
[Graphical view]
PANTHERiPTHR10046. PTHR10046. 2 hits.
PfamiPF05362. Lon_C. 1 hit.
PF01078. Mg_chelatase. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR00764. lon_rel. 1 hit.
PROSITEiPS51786. LON_PROTEOLYTIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O29883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEEVREILG GLDFESTKDV AVPERLIDQV IGQDHAVEAI KKAAVQKRHV
60 70 80 90 100
MLIGSPGTGK SMLAKAMAEL LPKEELEDIL VYPNPQDPNQ PKIRLVPAGK
110 120 130 140 150
GREIVEAYKE EAMKKAQARN FLIFTLVFLV IGYTVLTNPG NLIWGIIAAV
160 170 180 190 200
LILMMSRYFI PREDRNVPKL LVDNSDKVTA PFEDATGAHA GALFGDVRHD
210 220 230 240 250
PFQSGGLETP AHERVEAGAI HRAHKGVLYI DEINTLTIES QQKLLTALQD
260 270 280 290 300
KKFPITGQSE RSSGAMVRTE PVPCDFILVA AGNLDALMGM HPALRSRIEG
310 320 330 340 350
YGYEVYMNDT MPDTPENRQK LVRFVAQEVV KDGKIPHFDK YAVAEIIKEA
360 370 380 390 400
RRRAGRRNHL TLRLRELGGL VRTAGDIAKS EGSDIVRLEH VLKAKKIAKT
410 420 430 440 450
IEEQLADKYI ERRKDYKLFI TEGYEVGRVN GLAVIGESAG IVLPIIAEVT
460 470 480 490 500
PSMSKSEGRV IATGRLQEIA REAVMNVSAI IKKYTGRDIS NMDVHIQFVG
510 520 530 540 550
TYEGVEGDSA SISIATAVIS AIEGIPVDQS VAMTGSLSVK GEVLPVGGVT
560 570 580 590 600
QKIEAAIQAG LKKVIIPKDN IDDVLLDAEH EGKIEVIPVS RINEVLEHVL
610 620
EDGKKKNRLM SKFKELELAA V
Length:621
Mass (Da):68,208
Last modified:January 1, 1998 - v1
Checksum:iCC18C401C6799B3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90868.1.
PIRiD69295.
RefSeqiWP_010877871.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90868; AAB90868; AF_0364.
GeneIDi1483579.
KEGGiafu:AF_0364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90868.1.
PIRiD69295.
RefSeqiWP_010877871.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z0BX-ray1.55A415-621[»]
1Z0CX-ray1.55A415-621[»]
1Z0EX-ray2.05A/B/C/D/E/F417-621[»]
1Z0GX-ray2.27A/B/C/D/E/F417-621[»]
1Z0TX-ray3.00A/B/C/D/E/F417-621[»]
1Z0VX-ray3.00A/B/C/D/E/F417-621[»]
1Z0WX-ray1.20A415-621[»]
ProteinModelPortaliO29883.
SMRiO29883. Positions 416-621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF0364.

Protein family/group databases

MEROPSiS16.005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB90868; AAB90868; AF_0364.
GeneIDi1483579.
KEGGiafu:AF_0364.

Phylogenomic databases

eggNOGiarCOG02160. Archaea.
COG1067. LUCA.
KOiK04076.
OMAiDVHIQFV.

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-374-MONOMER.
BRENDAi3.4.21.53. 414.

Miscellaneous databases

EvolutionaryTraceiO29883.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR004663. Lon_arc.
IPR027065. Lon_Prtase.
IPR000523. Mg_chelatse_chII_dom.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR002078. Sigma_54_int.
[Graphical view]
PANTHERiPTHR10046. PTHR10046. 2 hits.
PfamiPF05362. Lon_C. 1 hit.
PF01078. Mg_chelatase. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR00764. lon_rel. 1 hit.
PROSITEiPS51786. LON_PROTEOLYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  2. "Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases."
    Botos I., Melnikov E.E., Cherry S., Kozlov S., Makhovskaya O.V., Tropea J.E., Gustchina A., Rotanova T.V., Wlodawer A.
    J. Mol. Biol. 351:144-157(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 415-621 OF WILD TYPE AND MUTANTS ALA-506 AND ALA-508, FUNCTION, MUTAGENESIS OF SER-509.

Entry informationi

Entry nameiLONB_ARCFU
AccessioniPrimary (citable) accession number: O29883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 109 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, Reference 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.