LONB_PYRHO
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 03-AUG-2022, entry version 140.
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}.
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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; 70601.3256855; -.
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 OMA; HDPFQCF; -.
DR OrthoDB; 7657at2157; -.
DR Proteomes; UP000000752; 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; 3.10.28.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR041699; AAA_32.
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; IPR004860; LAGLIDADG_2.
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; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55608; SSF55608; 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..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
