ID   LONB_PYRHO              Reviewed;        1127 AA.
AC   O58221;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Archaeal Lon protease;
DE            EC=3.4.21.-;
DE   AltName: Full=ATP-dependent protease La homolog;
DE   Contains:
DE     RecName: Full=Pho lon intein;
GN   OrderedLocusNames=PH0452;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000001; BAA29538.1; -; Genomic_DNA.
DR   PIR; E71156; E71156.
DR   RefSeq; WP_010884561.1; NC_000961.1.
DR   AlphaFoldDB; O58221; -.
DR   SMR; O58221; -.
DR   STRING; 70601.gene:9377383; -.
DR   MEROPS; S16.005; -.
DR   EnsemblBacteria; BAA29538; BAA29538; BAA29538.
DR   GeneID; 1444348; -.
DR   KEGG; pho:PH0452; -.
DR   eggNOG; arCOG02160; Archaea.
DR   eggNOG; arCOG03158; Archaea.
DR   OrthoDB; 64652at2157; -.
DR   Proteomes; UP000000752; Chromosome.
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 DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00081; Hint; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
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; IPR046843; LonB_AAA-LID.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR002078; Sigma_54_int.
DR   NCBIfam; TIGR01445; intein_Nterm; 1.
DR   NCBIfam; TIGR00764; lon_rel; 1.
DR   PANTHER; PTHR10046:SF46; ARCHAEAL LON PROTEASE; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF20436; LonB_AAA-LID; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF55608; Homing endonucleases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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..210
FT                   /note="Archaeal Lon protease, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026729"
FT   CHAIN           211..684
FT                   /note="Pho lon intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026730"
FT   CHAIN           685..1127
FT                   /note="Archaeal Lon protease, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026731"
FT   TOPO_DOM        1..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..1127
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          417..572
FT                   /note="DOD-type homing endonuclease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT   DOMAIN          904..1083
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          1103..1127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1107..1127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        990
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1033
FT                   /evidence="ECO:0000250"
FT   BINDING         59..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1127 AA;  126992 MW;  D756DD47332891E1 CRC64;
     MLSGESEMDE ERMDLGIEFE TTEEIPVPER LIDQVIGQDH AVEVIKTAAK QRRHVLLIGE
     PGTGKSMLGQ AMAELLPTEE LEDILVFPNP EDENMPRIKT VPAGQGRKIV EEYRRKAKEQ
     EGVRFYLLFF VFFIVAMAVF LSHGDPNTLL LGVFVILVAL MVTANMRFKT QAMVPKLLVD
     NSGRKRAPFV DATGAHAGAL LGDVRHDPFQ CFSGEEVIIV EKGKDRKVVK LREFVEDALK
     EPSGEGMDGD IKVTYKDLRG EDVRILTKDG FVKLLYVNKR EGKQKLRKIV NLDKDYWLAV
     TPDHKVFTSE GLKEAGEITE KDEIIRVPLV ILDGPKIAST YGEDGKFDDY IRWKKYYEKT
     GNGYKRAAKE LNIKESTLRW WTQGAKPNSL KMIEELEKLN LLPLTSEDSR LEKVAIILGA
     LFSDGNIDRN FNTLSFISSE RKAIERFVET LKELFGEFNY EIRDNHESLG KSILFRTWDR
     RIIRFFVALG APVGNKTKVK LELPWWIKLK PSLFLAFMDG LYSGDGSVPR FARYEEGIKF
     NGTFEIAQLT DDVEKKLPFF EEIAWYLSFF GIKAKVRVDK TGDKYKVRLI FSQSIDNVLN
     FLEFIPISLS PAKREKFLRE VESYLAAVPE SSLAGRIEEL REHFNRIKKG ERRSFIETWE
     VVNVTYNVTT ETGNLLANGL FVKNSGGLGT PAHLRVEPGM IHRAHKGVLF IDEIATLSLK
     MQQSLLTAMQ EKKFPITGQS ELSSGAMVRT EPVPCDFILV AAGNLDTIEK MHPALRSRIR
     GYGYEVYMRT TMPDTPENRR KLVQFVAQEV KKDGRIPHFT RDAVEEIVRE AQRRAGRKGH
     LTLRLRDLGG VVRAAGDIAV RKGKKYVTRE DVLEALKLAK PLEKQLADWY IERKKEYQVI
     RVEGGEIGRV NGLAIIGEQS GIVLPIEAIV APAASKEEGK IIVTGKLGEI AKEAVLNVSA
     IIKRYKGEDI SKYDIHVQFL QTYEGVEGDS ASISVATAVI SALEEIPVRQ DVAMTGSLSV
     RGEVLPVGGV TPKIEAAIEA GIKTVIIPKS NEKDVFLSPD KRKKIKIIPV ERIDEVLEVA
     LVESEKKREL IKRVRESLPL WMEETPSGET LHEHKGGATL PLEESKA
//