ID Q18DX8_HALWD Unreviewed; 749 AA.
AC Q18DX8;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
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 Name=lon {ECO:0000313|EMBL:CAJ51293.1};
GN OrderedLocusNames=HQ_1163A {ECO:0000313|EMBL:CAJ51293.1};
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ51293.1, ECO:0000313|Proteomes:UP000001975};
RN [1] {ECO:0000313|EMBL:CAJ51293.1, ECO:0000313|Proteomes:UP000001975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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}.
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; AM180088; CAJ51293.1; -; Genomic_DNA.
DR RefSeq; WP_011570458.1; NC_008212.1.
DR AlphaFoldDB; Q18DX8; -.
DR STRING; 362976.HQ_1163A; -.
DR GeneID; 4194230; -.
DR KEGG; hwa:HQ_1163A; -.
DR eggNOG; arCOG02160; Archaea.
DR HOGENOM; CLU_392630_0_0_2; -.
DR Proteomes; UP000001975; 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; 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:UP000001975};
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 235..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369001"
FT DOMAIN 248..413
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 535..713
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 749 AA; 80775 MW; DB071F4EE178A074 CRC64;
MSNDTDSDEN PPAEGSGFTD ETPDSSQHGD DGLSEEHANA EAGTDTDTGA NAGADGRSDD
SGREDHDDRG DRDRGHDSYN DSVDTVDPDG PTDRENGSIE ELGSDVEVDA EVKDDVDEDD
LLGGLKISST AEIDVPDRLV DQVIGQEHAR DVVMKAAKQR RHVMMIGSPG TGKSMLAKAM
SELLPKEELQ DVLVYHNPDD GNNPKVRTVP AGKGDQIVDA HKEEARKRNQ MRSFLMWIII
AIVLGYSLII AGQILLGILA AGVIYLAFRY GSRGGDAMIP NLIVNNADTA TAPFEDATGA
HAGALLGDVR HDPFQSGGME TPSHDRVEPG SIHKANKGVL YIDEINTLDI RSQQHLMTAI
QEGEFSITGQ SERSSGAMVQ TEAVPTDFIM IAAGNLDAME NMHPALRSRI KGYGYEVYMD
DTIEDTPDMR RKYTRFIAQE VNKDGRLPDY NAEAIEEIIL EARRRAGRKG HLTLELRNLG
GLVRVAGDIA RAADADYVRR DHVLQAKGRS RSIEQQLADD YIERRKDYEL QVSDGYQAGR
VNGLAVMGED SGIMLPVMAE VTPSQGPGQV IATGQLKEMA QEAVDNVSAI IKKFSDENIS
EKDMHIQFVQ TGQQGVDGDS ASITVATAVI SALENVGVDQ SLAMTGSLSV RGDVLPVGGV
THKIEAAAKS GCERIIIPAA NSQDVMIEEE YEEMVEIIPV SHISEVLDIA LEGEAEKDSL
VARLKSITGS ALSQSKNETV SGPSNPSPQ
//
