ID A0A1I0NY48_9EURY Unreviewed; 694 AA.
AC A0A1I0NY48;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=SAMN04487945_1239 {ECO:0000313|EMBL:SEW06699.1};
OS Halobacterium jilantaiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=355548 {ECO:0000313|EMBL:SEW06699.1, ECO:0000313|Proteomes:UP000198518};
RN [1] {ECO:0000313|EMBL:SEW06699.1, ECO:0000313|Proteomes:UP000198518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5337 {ECO:0000313|EMBL:SEW06699.1,
RC ECO:0000313|Proteomes:UP000198518};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU369001}.
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DR EMBL; FOJA01000001; SEW06699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0NY48; -.
DR STRING; 355548.SAMN04487945_1239; -.
DR OrthoDB; 64652at2157; -.
DR Proteomes; UP000198518; Unassembled WGS sequence.
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; IPR046843; LonB_AAA-LID.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
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; PF20436; LonB_AAA-LID; 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.
DR PROSITE; PS01046; LON_SER; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198518};
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 177..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369001"
FT DOMAIN 191..356
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 478..658
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 565
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 608
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 694 AA; 75530 MW; 7E8E027A254D9815 CRC64;
MSNESTKDAP RPDDPDDPED QGHGPREGPD PDVRDDVEDL EDLGSDVGVE GDVSINEEDA
EDDLLGGLKI GDTSDIKVPD RLVDQVIGQE AAREIVMRAA KQHRHVMMIG SPGTGKSLLA
KAMSHLLPKE SLQDVLVYHN PDDSNEPKVR TVPAGKGEQI VEAHQEEARK RNQMRSFLMW
IIILLVVGYA LLMARQPLLG IIAAGAIYLV FRYSNRGSDA MVPKLLINNA DRQVAPFEDA
TGAHAGAMLG DVRHDPFQSG GMETPSHDRV EAGSIQKANK GVLFIDEINT LDVRSQQKLM
TAIQEGEFSI TGQSERSSGA MVQTEPVPCD FIMVAAGNMD AMENMHPALR SRIKGYGYEV
YMDDTIEDTP EMRRKYARFV AQEVEKDGNL PHFHPEAVRE LILEAKRRAG RKDHLTLKLR
DLGGLVRVAG DIARSEGHDL TQREDVLEAK KRSRSIEQQF VDNYIERRKD YELGTSNEEA
VGRVNGLAVM GGDSGIMLPV MAEITPAQSQ EEGRIYATGQ LQEMAEEAVE NVSAIIKKFS
DENMSEKDTH IQFVQAGEGG VDGDSASITV ATAVISALED IPVAQDLAMT GSLSVRGDVL
PVGGVTHKIE AAAKAGCKRV IIPKANENDV MIEDEYEEQI EIIPVSHISE VLDVALVGEP
EKDSLVDRLK SITGKALEGS TDSGTATGGS PSPQ
//
