LONB_PYRAB
ID LONB_PYRAB Reviewed; 998 AA.
AC Q9UYC6; G8ZJ07;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, 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;
DE Contains:
DE RecName: Full=Pab lon intein;
GN Name=lon; OrderedLocusNames=PYRAB15820; ORFNames=PAB1313;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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}.
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 -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ248288; CAB50486.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71040.1; -; Genomic_DNA.
DR PIR; H75005; H75005.
DR AlphaFoldDB; Q9UYC6; -.
DR SMR; Q9UYC6; -.
DR STRING; 272844.PAB1313; -.
DR MEROPS; S16.005; -.
DR EnsemblBacteria; CAB50486; CAB50486; PAB1313.
DR KEGG; pab:PAB1313; -.
DR PATRIC; fig|272844.11.peg.1687; -.
DR eggNOG; arCOG02160; Archaea.
DR eggNOG; arCOG03158; Archaea.
DR HOGENOM; CLU_281280_0_0_2; -.
DR OMA; HDPFQCF; -.
DR PhylomeDB; Q9UYC6; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
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; IPR041699; AAA_32.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
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; 2.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR TIGRFAMs; TIGR00764; lon_rel; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Autocatalytic cleavage; Cell membrane; Endonuclease;
KW Hydrolase; Intron homing; Membrane; Nuclease; Nucleotide-binding; Protease;
KW Protein splicing; Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..220
FT /note="Archaeal Lon protease, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026726"
FT CHAIN 221..553
FT /note="Pab lon intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026727"
FT CHAIN 554..998
FT /note="Archaeal Lon protease, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026728"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..998
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 370..496
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT DOMAIN 773..952
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 971..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 859
FT /evidence="ECO:0000250"
FT ACT_SITE 902
FT /evidence="ECO:0000250"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 998 AA; 111704 MW; BDB15A8B00D135F9 CRC64;
MLKFYKMGIK RLSGEMTMGE ERMDLGIEFE TTEEIPVPER LIDQVIGQDH AVEVIKTAAK
QRRHVLLIGE PGTGKSMLGQ AMAELLPTED LEDILVFPNP EDENMPRIKT VPAGQGRRIV
EEYKRKAKEQ ENIRFYLLFF VFFIVAMAVF MSRGDPNTLL LGVFVILIAL MVTANMRFRT
QAMVPKLLVD NSGRKRAPFV DATGAHAGAL LGDVRHDPFQ CFSGEETVVI RENGEVKVLR
LKDFVEKALE KPSGEGLDGD VKVVYHDFRN ENVEVLTKDG FTKLLYANKR IGKQKLRRVV
NLEKDYWFAL TPDHKVYTTD GLKEAGEITE KDELISVPIT VFDCEDEDLK KIGLLPLTSD
DERLRKIATL MGILFNGGSI DEGLGVLTLK SERSVIEKFV ITLKELFGKF EYEIIKEENT
ILKTRDPRII KFLVGLGAPI EGKDLKMPWW VKLKPSLFLA FLEGFRAHIV EQLVDDPNKN
LPFFQELSWY LGLFGIKADI KVEEVGDKHK IIFDAGRLDV DKQFIETWED VEVTYNLTTE
KGNLLANGLF VKNSGGLGTP AHLRVEPGMI HRAHKGVLFI DEIATLSLKM QQSLLTAMQE
KKFPITGQSE LSSGAMVRTE PVPCDFILVA AGNLDTIEKM HPALRSRIRG YGYEVYMRTT
MPDTVENRRK LVQFVAQEVK KDGRIPHFTR DAVEEIIREA QRRAGRKGHL TLRLRDLGGV
VRAAGDIAVR KGKKYVTRED VLEALQMAKP LEKQLADWYI ERKKEYQVIR TEGGEIGRVN
GLAIIGEQSG IVLPIEAIVA PAASKEEGKI IVTGKLGEIA REAVLNVSAI IKRYKGEDIS
RYDIHVQFLQ TYEGVEGDSA SISVATAVIS ALEEIPVRQD VAMTGSLSVR GEVLPVGGVT
PKIEAAIEAG IKKVIIPKAN EKDVFLSPDK REKIEIIPVE RIDEVLEVAL VESEKKKELI
KRIRETLPLG VSESAGSETL HEHGRDSGSA LSVEESKA
