ID M0AKD5_NATA1 Unreviewed; 747 AA.
AC M0AKD5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=C481_16507 {ECO:0000313|EMBL:ELY98821.1};
OS Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS P-10747 / NBRC 102637 / 172P1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=29540 {ECO:0000313|EMBL:ELY98821.1, ECO:0000313|Proteomes:UP000011554};
RN [1] {ECO:0000313|EMBL:ELY98821.1, ECO:0000313|Proteomes:UP000011554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12278 {ECO:0000313|EMBL:ELY98821.1,
RC ECO:0000313|Proteomes:UP000011554};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY98821.1}.
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DR EMBL; AOIO01000036; ELY98821.1; -; Genomic_DNA.
DR RefSeq; WP_006110387.1; NZ_AOIO01000036.1.
DR AlphaFoldDB; M0AKD5; -.
DR STRING; 29540.C481_16507; -.
DR PATRIC; fig|29540.5.peg.3363; -.
DR eggNOG; arCOG02160; Archaea.
DR OrthoDB; 64652at2157; -.
DR Proteomes; UP000011554; 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 CDD; cd00009; AAA; 1.
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; 1.
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.
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:UP000011554};
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 234..267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369001"
FT DOMAIN 534..712
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 619
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 747 AA; 81462 MW; CB11F653E7BF4994 CRC64;
MSNDTNADDP PEDASGTVPR EEQAQDEERE RGRESERVQD GRDRERSPQT PSHPESTPQS
QSQSTERQGE RSPTDGDEDT AGDGNRRDEA DDIETVDDLG SSVEVDPGVE VDDEIAEDDL
LGGLKIDSTE DIEVPDRLVD QVIGQDEARD IIIKAAKQRR HVMMIGSPGT GKSMLAKAMS
QLLPKEELQD VLVYHNPDDG NEPKVRTVPA GKGEQIIDAH KEEARKRNQM RSILMWIIIA
VIIGYAIISP VSPLLGILAA GIIWLIFRYT SRGTDAMVPN MIVNNGDKRT APFEDATGAH
AGALLGDVRH DPFQSGGMET PSHDRVEPGS IHKSNKGVLF VDEINTLDVR TQQKLMTAIQ
EGEFSITGQS ERSSGAMVQT EPVPCDFVMI AAGNLDAMEN MHPALRNRIK GYGYEVYMDD
TIEDTPEMRR KYARFIAQEV ERDGRLPHFT HEAVEELLLE AKRRSGRKNH LTLHFRSLGG
LIRVAGDIAR AEDRDLTTRD DVLQAKGRSR SIEQQLADDY IERRKDYELQ VTEDGVEGRV
NGLAVMGEDS GIMLPVMAEI APAQGGGQVI ATGKLQEMAE ESVQNVSAII KKFSDVDLSE
KDIHIQFVQA GQQGVDGDSA SITVATAVIS ALENIPVDQS IAMTGSLSVR GDVLPVGGVT
HKIEAAAKAG CNTVIIPAAN EQDVMIEDEY EEMIDIVPCS NISEVLDVAL EGEPEKDSLL
DRLKSITGTA FEQQSVGSAG GSNPSPQ
//
