LONB_ARCFU
ID LONB_ARCFU Reviewed; 621 AA.
AC O29883;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Archaeal Lon protease;
DE EC=3.4.21.-;
DE AltName: Full=ATP-dependent protease La homolog;
GN OrderedLocusNames=AF_0364;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 415-621 OF WILD TYPE AND MUTANTS
RP ALA-506 AND ALA-508, FUNCTION, AND MUTAGENESIS OF SER-509.
RX PubMed=16002085; DOI=10.1016/j.jmb.2005.06.008;
RA Botos I., Melnikov E.E., Cherry S., Kozlov S., Makhovskaya O.V.,
RA Tropea J.E., Gustchina A., Rotanova T.V., Wlodawer A.;
RT "Atomic-resolution crystal structure of the proteolytic domain of
RT Archaeoglobus fulgidus lon reveals the conformational variability in the
RT active sites of lon proteases.";
RL J. Mol. Biol. 351:144-157(2005).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of mutant and abnormal proteins as well as certain short-
CC lived regulatory proteins. Degrades polypeptides processively (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16002085}.
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000782; AAB90868.1; -; Genomic_DNA.
DR PIR; D69295; D69295.
DR RefSeq; WP_010877871.1; NC_000917.1.
DR PDB; 1Z0B; X-ray; 1.55 A; A=415-621.
DR PDB; 1Z0C; X-ray; 1.55 A; A=415-621.
DR PDB; 1Z0E; X-ray; 2.05 A; A/B/C/D/E/F=417-621.
DR PDB; 1Z0G; X-ray; 2.27 A; A/B/C/D/E/F=417-621.
DR PDB; 1Z0T; X-ray; 3.00 A; A/B/C/D/E/F=417-621.
DR PDB; 1Z0V; X-ray; 3.00 A; A/B/C/D/E/F=417-621.
DR PDB; 1Z0W; X-ray; 1.20 A; A=415-621.
DR PDBsum; 1Z0B; -.
DR PDBsum; 1Z0C; -.
DR PDBsum; 1Z0E; -.
DR PDBsum; 1Z0G; -.
DR PDBsum; 1Z0T; -.
DR PDBsum; 1Z0V; -.
DR PDBsum; 1Z0W; -.
DR AlphaFoldDB; O29883; -.
DR SMR; O29883; -.
DR STRING; 224325.AF_0364; -.
DR MEROPS; S16.005; -.
DR EnsemblBacteria; AAB90868; AAB90868; AF_0364.
DR GeneID; 1483579; -.
DR KEGG; afu:AF_0364; -.
DR eggNOG; arCOG02160; Archaea.
DR HOGENOM; CLU_392630_0_0_2; -.
DR OMA; GLYFWNL; -.
DR OrthoDB; 7657at2157; -.
DR PhylomeDB; O29883; -.
DR BRENDA; 3.4.21.53; 414.
DR EvolutionaryTrace; O29883; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR004663; Lon_arc.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR002078; Sigma_54_int.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00764; lon_rel; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Protease; Reference proteome; Serine protease;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..621
FT /note="Archaeal Lon protease"
FT /id="PRO_0000076151"
FT TOPO_DOM 1..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 423..602
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 506
FT /note="E->A: Slightly decreases proteolytic activity."
FT MUTAGEN 508
FT /note="D->A: No effect."
FT MUTAGEN 509
FT /note="S->A: Completely abolishes proteolytic activity."
FT /evidence="ECO:0000269|PubMed:16002085"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:1Z0W"
FT STRAND 428..435
FT /evidence="ECO:0007829|PDB:1Z0W"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:1Z0W"
FT STRAND 439..451
FT /evidence="ECO:0007829|PDB:1Z0W"
FT HELIX 467..485
FT /evidence="ECO:0007829|PDB:1Z0W"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:1Z0W"
FT STRAND 492..500
FT /evidence="ECO:0007829|PDB:1Z0W"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:1Z0G"
FT HELIX 512..523
FT /evidence="ECO:0007829|PDB:1Z0W"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:1Z0W"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:1Z0W"
FT HELIX 549..558
FT /evidence="ECO:0007829|PDB:1Z0W"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:1Z0W"
FT HELIX 568..573
FT /evidence="ECO:0007829|PDB:1Z0W"
FT TURN 578..582
FT /evidence="ECO:0007829|PDB:1Z0W"
FT STRAND 583..591
FT /evidence="ECO:0007829|PDB:1Z0W"
FT HELIX 592..599
FT /evidence="ECO:0007829|PDB:1Z0W"
FT HELIX 604..620
FT /evidence="ECO:0007829|PDB:1Z0W"
SQ SEQUENCE 621 AA; 68208 MW; CC18C401C6799B3A CRC64;
MNEEVREILG GLDFESTKDV AVPERLIDQV IGQDHAVEAI KKAAVQKRHV MLIGSPGTGK
SMLAKAMAEL LPKEELEDIL VYPNPQDPNQ PKIRLVPAGK GREIVEAYKE EAMKKAQARN
FLIFTLVFLV IGYTVLTNPG NLIWGIIAAV LILMMSRYFI PREDRNVPKL LVDNSDKVTA
PFEDATGAHA GALFGDVRHD PFQSGGLETP AHERVEAGAI HRAHKGVLYI DEINTLTIES
QQKLLTALQD KKFPITGQSE RSSGAMVRTE PVPCDFILVA AGNLDALMGM HPALRSRIEG
YGYEVYMNDT MPDTPENRQK LVRFVAQEVV KDGKIPHFDK YAVAEIIKEA RRRAGRRNHL
TLRLRELGGL VRTAGDIAKS EGSDIVRLEH VLKAKKIAKT IEEQLADKYI ERRKDYKLFI
TEGYEVGRVN GLAVIGESAG IVLPIIAEVT PSMSKSEGRV IATGRLQEIA REAVMNVSAI
IKKYTGRDIS NMDVHIQFVG TYEGVEGDSA SISIATAVIS AIEGIPVDQS VAMTGSLSVK
GEVLPVGGVT QKIEAAIQAG LKKVIIPKDN IDDVLLDAEH EGKIEVIPVS RINEVLEHVL
EDGKKKNRLM SKFKELELAA V
