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Archaeal Lon protease (EC 3.4.21.-) (ATP-dependent protease La homolog) [Cleaved into: Pab lon intein]

 LONB_PYRAB              Reviewed;         998 AA.
Q9UYC6; G8ZJ07;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-JUN-2017, entry version 119.
RecName: Full=Archaeal Lon protease;
EC=3.4.21.-;
AltName: Full=ATP-dependent protease La homolog;
Contains:
RecName: Full=Pab lon intein;
Name=lon; OrderedLocusNames=PYRAB15820; ORFNames=PAB1313;
Pyrococcus abyssi (strain GE5 / Orsay).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=272844;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GE5 / Orsay;
PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C.,
Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
"An integrated analysis of the genome of the hyperthermophilic
archaeon Pyrococcus abyssi.";
Mol. Microbiol. 47:1495-1512(2003).
[2]
GENOME REANNOTATION.
STRAIN=GE5 / Orsay;
PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
Gao J., Wang J.;
"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5
and Pyrococcus furiosus DSM 3638.";
Curr. Microbiol. 64:118-129(2012).
-!- FUNCTION: 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). {ECO:0000250}.
-!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000305}.
-!- PTM: This protein undergoes a protein self splicing that involves
a post-translational excision of the intervening region (intein)
followed by peptide ligation. {ECO:0000305}.
-!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ248288; CAB50486.1; -; Genomic_DNA.
EMBL; HE613800; CCE71040.1; -; Genomic_DNA.
PIR; H75005; H75005.
ProteinModelPortal; Q9UYC6; -.
SMR; Q9UYC6; -.
STRING; 272844.PAB1313; -.
MEROPS; S16.005; -.
EnsemblBacteria; CAB50486; CAB50486; PAB1313.
KEGG; pab:PAB1313; -.
PATRIC; fig|272844.11.peg.1687; -.
eggNOG; arCOG02160; Archaea.
eggNOG; arCOG03158; Archaea.
eggNOG; COG1067; LUCA.
eggNOG; COG1372; LUCA.
HOGENOM; HOG000113346; -.
KO; K04076; -.
OMA; DPFQCFS; -.
OrthoDB; POG093Z00OX; -.
Proteomes; UP000000810; Chromosome.
Proteomes; UP000009139; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008134; F:transcription factor binding; IEA:InterPro.
GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
Gene3D; 3.30.230.10; -; 1.
InterPro; IPR028992; Hedgehog/Intein_dom.
InterPro; IPR003587; Hint_dom_N.
InterPro; IPR030934; Intein_C.
InterPro; IPR004042; Intein_endonuc.
InterPro; IPR006141; Intein_N.
InterPro; IPR004663; Lon_arc.
InterPro; IPR008269; Lon_proteolytic.
InterPro; IPR027065; Lon_Prtase.
InterPro; IPR000523; Mg_chelatse_chII_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
InterPro; IPR002078; Sigma_54_int.
PANTHER; PTHR10046; PTHR10046; 1.
Pfam; PF05362; Lon_C; 1.
Pfam; PF01078; Mg_chelatase; 1.
SMART; SM00306; HintN; 1.
SUPFAM; SSF51294; SSF51294; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54211; SSF54211; 1.
TIGRFAMs; TIGR01445; intein_Nterm; 1.
TIGRFAMs; TIGR00764; lon_rel; 1.
PROSITE; PS50818; INTEIN_C_TER; 1.
PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
PROSITE; PS50817; INTEIN_N_TER; 1.
PROSITE; PS51786; LON_PROTEOLYTIC; 1.
3: Inferred from homology;
ATP-binding; Autocatalytic cleavage; Cell membrane; Complete proteome;
Endonuclease; Hydrolase; Intron homing; Membrane; Nuclease;
Nucleotide-binding; Protease; Protein splicing; Serine protease;
Transmembrane; Transmembrane helix.
CHAIN 1 220 Archaeal Lon protease, 1st part.
{ECO:0000255}.
/FTId=PRO_0000026726.
CHAIN 221 553 Pab lon intein. {ECO:0000255}.
/FTId=PRO_0000026727.
CHAIN 554 998 Archaeal Lon protease, 2nd part.
{ECO:0000255}.
/FTId=PRO_0000026728.
TOPO_DOM 1 131 Cytoplasmic. {ECO:0000255}.
TRANSMEM 132 152 Helical. {ECO:0000255}.
TOPO_DOM 153 155 Extracellular. {ECO:0000255}.
TRANSMEM 156 176 Helical. {ECO:0000255}.
TOPO_DOM 177 998 Cytoplasmic. {ECO:0000255}.
DOMAIN 370 496 DOD-type homing endonuclease.
{ECO:0000255|PROSITE-ProRule:PRU00273}.
DOMAIN 773 952 Lon proteolytic. {ECO:0000255|PROSITE-
ProRule:PRU01122}.
NP_BIND 69 76 ATP. {ECO:0000255}.
ACT_SITE 859 859 {ECO:0000250}.
ACT_SITE 902 902 {ECO:0000250}.
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


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