UniProt: L0JQS6

Database: UniProt
Entry: L0JQS6_NATP1

LinkDB:  L0JQS6_NATP1 
Original site:  L0JQS6_NATP1

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Ontology (8)   
   GO (8)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (20)   
   InterPro (11)   
   Pfam (5)   
   PROSITE (3)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (34)   

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ID   L0JQS6_NATP1            Unreviewed;       718 AA.
AC   L0JQS6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=Natpe_2934 {ECO:0000313|EMBL:AGB32731.1};
GN   ORFNames=C488_08787 {ECO:0000313|EMBL:ELY75733.1};
OS   Natrinema pellirubrum (strain DSM 15624 / CIP 106293 / JCM 10476 / NCIMB
OS   786 / 157).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=797303 {ECO:0000313|EMBL:AGB32731.1, ECO:0000313|Proteomes:UP000010843};
RN   [1] {ECO:0000313|EMBL:AGB32731.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 15624 {ECO:0000313|EMBL:AGB32731.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT   "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000010843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15624 / JCM 10476 / NCIMB 786
RC   {ECO:0000313|Proteomes:UP000010843};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT   "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000011593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15624 {ECO:0000313|Proteomes:UP000011593};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ELY75733.1, ECO:0000313|Proteomes:UP000011593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15624 {ECO:0000313|EMBL:ELY75733.1,
RC   ECO:0000313|Proteomes:UP000011593};
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}.
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DR   EMBL; CP003372; AGB32731.1; -; Genomic_DNA.
DR   EMBL; AOIE01000062; ELY75733.1; -; Genomic_DNA.
DR   RefSeq; WP_006181123.1; NZ_AOIE01000062.1.
DR   AlphaFoldDB; L0JQS6; -.
DR   STRING; 797303.Natpe_2934; -.
DR   GeneID; 14333514; -.
DR   KEGG; npe:Natpe_2934; -.
DR   PATRIC; fig|797303.5.peg.1757; -.
DR   eggNOG; arCOG02160; Archaea.
DR   HOGENOM; CLU_392630_0_0_2; -.
DR   OrthoDB; 64652at2157; -.
DR   Proteomes; UP000010843; Chromosome.
DR   Proteomes; UP000011593; 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};
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        205..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369001"
FT   DOMAIN          214..383
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   DOMAIN          505..683
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..70
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        590
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        633
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   718 AA;  77855 MW;  86C24F792C03BE74 CRC64;
     MSENTNGGDP PEDASEPAPT DERPEEPAER QGDRSSPEDE SGRRDSADDP IDGVDPSSDE
     DDDLETVEDL GSTVEVDPGV EVDEEIAEDD LLGGLKIDTT EDIEVPERLV DQVIGQDEAR
     DIIIKAAKQR RHVMMIGSPG TGKSMLAKAM SQLLPKEDLQ DVLVYPNPDD ENEPKVRTVP
     AGKGDQIVDA HKEEASKRNR MRSILMWVVI AVILAYTILS GSSLLLGLLA AGVIWFIFRT
     LGQGSDAMVP NLLVNNGDQR VAPFEDATGA HAGALLGDVR HDPFQSGGMG TPSHERVEPG
     SIHQSNKGVL FLDEINTLDI QTQQKLMTAI QEGEFSITGQ SERSSGAMVQ TEPVPCDFIM
     VAAGNLDAME NMHPALRNRI KGYGYEVYMD DTIEDTPEMR RKYARFIAQE VERDGRLPHF
     TDDAVEELIL EAKRRSGRKN HLTLHFRTLG GLVRVAGDIA RAEDREHTTR DDVLRAKDRS
     RSIEQQLADD YIERRKDYEL QITKDGVAGR VNGLAVMGED SGIMLPVMAE IAPTQGGGRV
     IATGQLKEMA EESVQNVSAI IKKFSDVDLS EKDIHIQFVQ AGEGGVDGDS ASITVATAVI
     SALEDIPVDQ SVAMTGSLSV RGDVLPVGGV THKIEAAAKA GCTKVIIPEA NEQDVMIEDE
     YEDMIEIIPC SHISEVLDVA LMGEPKKDSL VARLRSITGT AFEQEAVGSA SGSSPSPQ
//

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