ID D3S3Y5_METSF Unreviewed; 655 AA.
AC D3S3Y5;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Archaeal Lon protease {ECO:0000256|ARBA:ARBA00022016, ECO:0000256|RuleBase:RU369001};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU369001};
DE AltName: Full=ATP-dependent protease La homolog {ECO:0000256|RuleBase:RU369001};
GN OrderedLocusNames=MFS40622_0867 {ECO:0000313|EMBL:ADC69549.1};
OS Methanocaldococcus sp. (strain FS406-22).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=644281 {ECO:0000313|EMBL:ADC69549.1, ECO:0000313|Proteomes:UP000002189};
RN [1] {ECO:0000313|EMBL:ADC69549.1, ECO:0000313|Proteomes:UP000002189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS406-22 {ECO:0000313|EMBL:ADC69549.1,
RC ECO:0000313|Proteomes:UP000002189};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Leigh J.,
RA Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus sp. FS406-22.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU369001}.
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|ARBA:ARBA00026070, ECO:0000256|RuleBase:RU369001}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU369001}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU369001}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC subfamily. {ECO:0000256|ARBA:ARBA00009579,
CC ECO:0000256|RuleBase:RU369001}.
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DR EMBL; CP001901; ADC69549.1; -; Genomic_DNA.
DR RefSeq; WP_012980458.1; NC_013887.1.
DR AlphaFoldDB; D3S3Y5; -.
DR STRING; 644281.MFS40622_0867; -.
DR MEROPS; S16.008; -.
DR GeneID; 8804710; -.
DR KEGG; mfs:MFS40622_0867; -.
DR eggNOG; arCOG02160; Archaea.
DR HOGENOM; CLU_392630_0_0_2; -.
DR OrthoDB; 64652at2157; -.
DR Proteomes; UP000002189; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR002078; Sigma_54_int.
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; PF01078; Mg_chelatase; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU369001};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU369001};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369001};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369001};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU369001};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU369001}.
FT TRANSMEM 113..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369001"
FT TRANSMEM 138..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369001"
FT DOMAIN 456..639
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 550
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 593
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 655 AA; 72640 MW; 96110F498D2EA73D CRC64;
MFSIKFKTTE ELPEPSPRLI DQVIGQEEAV KIVLSAVKNK RNVILLGEPG VGKSMIVKAV
GEILSDFGEF TPYYVIAKPN LKNMERPIVE VIDGEYKEDL KEMPKLDLKT PSSTTLLLIM
IGAILLSEYL LKYLPQNYLL AAVTITALIV LIFGFVVILT SIMGASRASM PNNLNPMDLK
PVLLYECKKR PLVRASAYNV TRLLGDIKHC PLGGRPPLGT PPHKRIILGA IHEAHRGILY
VDEIKTMPLE VQDYILTALQ DKQLPISGRN PNSSGATVET NPIPCDFILI MSGNMDDVYN
LRAPLLDRID YKIVLKNKMD NTLENRDKLL QFIVQEIKNN NLNPMTYDGC CEVVRIAQYL
AGSKDKLTLR LRLLANIIKM ANDVAMGRDV EELLGNFDEK GNYNPETQKD KNNKVYITAE
HVRKVFDTGI YSMEKQVALN YIKNFKRYKH IVPNDEPKVG VVYGLAVLGA GGIGDVTKII
VQILESKNPG THLLNISGDI AKHSITLASA LSKKLVAEKK LPLPKKDIDL NNKEIYIQFS
QSYSKIDGDS ATAAVCLAII SALLNIPLKQ DFAITGSLDL SGNVLAIGGV NEKIEAAKRY
GFKRVIIPEA NMIDVIETGG IEIIPVKTLD EIIPLVFDLD SIDKNKSEKT EQVNK
//
