ID   LONB_HALSA              Reviewed;         702 AA.
AC   Q9HSC3;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Archaeal Lon protease;
DE            EC=3.4.21.-;
DE   AltName: Full=ATP-dependent protease La homolog;
GN   OrderedLocusNames=VNG_0303G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE004437; AAG18884.1; -; Genomic_DNA.
DR   PIR; H84189; H84189.
DR   RefSeq; WP_010902178.1; NC_002607.1.
DR   AlphaFoldDB; Q9HSC3; -.
DR   SMR; Q9HSC3; -.
DR   STRING; 64091.VNG_0303G; -.
DR   MEROPS; S16.A11; -.
DR   PaxDb; Q9HSC3; -.
DR   EnsemblBacteria; AAG18884; AAG18884; VNG_0303G.
DR   GeneID; 5952472; -.
DR   GeneID; 62885996; -.
DR   KEGG; hal:VNG_0303G; -.
DR   PATRIC; fig|64091.14.peg.223; -.
DR   HOGENOM; CLU_392630_0_0_2; -.
DR   InParanoid; Q9HSC3; -.
DR   OMA; GLYFWNL; -.
DR   OrthoDB; 7657at2157; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041699; AAA_32.
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; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR002078; Sigma_54_int.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF13654; AAA_32; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR00764; lon_rel; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR   PROSITE; PS01046; LON_SER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Hydrolase; Membrane; Nucleotide-binding;
KW   Protease; Reference proteome; Serine protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..702
FT                   /note="Archaeal Lon protease"
FT                   /id="PRO_0000076152"
FT   TOPO_DOM        1..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        224..702
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          487..667
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..63
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        574
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10087"
FT   ACT_SITE        617
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10087"
FT   BINDING         117..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   702 AA;  76017 MW;  203624C9836B2736 CRC64;
     MSNESTNDAP PDDDPDDPEP SVDHDDTDGL QDDPADSVDD AGEVDDLENL GSDVGVEGDV
     SIDEDNAEDD LLGGLRIDDT SDITVPDRLV DQVIGQEAAR EIVKRAAKQH RHVMMIGSPG
     TGKSLLAKAM SRLLPKESLQ DVLVYHNPDD SNEPKVRTVP AGKGEQIVDA HKEEARKRNQ
     MRSFLMWIMI LLAVGYALLI ATPARPLLAL LSAAGIYLLF RYTNRGSDAM VPKLLINNAD
     RQVAPFEDAT GAHAGAMLGD VRHDPFQSGG MATPSHERVE AGSIQKANKG VLFIDEINTL
     DVRSQQKLMT AIQEGEFSIT GQSERSSGAM VQTEAVPCDF IMVAAGNMDA MENMHPALRS
     RIKGYGYEVY MDDTIEDTPD MRRKYARFVA QEVEKDGNLP HFAPDAIREL ILEAKRRAGR
     KDSLTLKLRD LGGLVRVAGD IARSEGHDLT QRSDVLEAKK RSRSIEQQFV DNYIQRRKDY
     ELGTTSEEAV GRVNGLAVMG GDSGIMLPVM AEITPAQSQE EGRIYATGQL KEMAEEAVEN
     VSAIIKKFSD ENMSEKDTHI QFVQAGEGGV DGDSASITVA TAVISALEDI PVAQELAMTG
     SLSVRGDVLP VGGVTHKIEA AAKAGCERVI IPKANEDDVM IEDEYEEQIE IIPVTHISEV
     LDVALVGEPE KDSLVDRLKS ITGKALDSAS DSGTTGGNPS PQ