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Database: UniProt
Entry: H2J7X0_MARPK
LinkDB: H2J7X0_MARPK
Original site: H2J7X0_MARPK 
ID   H2J7X0_MARPK            Unreviewed;       792 AA.
AC   H2J7X0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   OrderedLocusNames=Marpi_1049 {ECO:0000313|EMBL:AEX85461.1};
OS   Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3).
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Marinitoga.
OX   NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX85461.1, ECO:0000313|Proteomes:UP000007161};
RN   [1] {ECO:0000313|EMBL:AEX85461.1, ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RX   PubMed=23045491; DOI=10.1128/JB.01430-12;
RA   Lucas S., Han J., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N.C., Ivanova N., Pagani I., Vannier P.,
RA   Oger P., Bartlett D.H., Noll K.M., Woyke T., Jebbar M.;
RT   "Complete Genome Sequence of the Thermophilic, Piezophilic, Heterotrophic
RT   Bacterium Marinitoga piezophila KA3.";
RL   J. Bacteriol. 194:5974-5975(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M.,
RA   Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.;
RT   "Complete sequence of chromosome of Marinitoga piezophila KA3.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01122};
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01122}.
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DR   EMBL; CP003257; AEX85461.1; -; Genomic_DNA.
DR   RefSeq; WP_014296533.1; NC_016751.1.
DR   AlphaFoldDB; H2J7X0; -.
DR   STRING; 443254.Marpi_1049; -.
DR   KEGG; mpz:Marpi_1049; -.
DR   eggNOG; COG1067; Bacteria.
DR   HOGENOM; CLU_014785_0_1_0; -.
DR   Proteomes; UP000007161; Chromosome.
DR   GO; GO:0005524; F:ATP binding; 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:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR041699; AAA_32.
DR   InterPro; IPR046844; Lon-like_helical.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR046843; LonB_AAA-LID.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046:SF46; ARCHAEAL LON PROTEASE; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   Pfam; PF13654; AAA_32; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF20436; LonB_AAA-LID; 1.
DR   Pfam; PF20437; LonC_helical; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000007161};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          551..747
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        642
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        685
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   792 AA;  91422 MW;  C7D2AC4A95138E21 CRC64;
     MLLKYDDFKI KMPQLNFENT ENIQSITEYI GQKRAYDSMV LGIEIEEKTH NIFITGPVNT
     GRRTFARNVL TKYSLNKKTP NDYIYVYNFK DPMKPKAISL KSGEAIIFKK ILKETIEISF
     EALKKGIEGE DFSEKRTQLE DEYLKARKSV WDDLKKEVEK LGFKLQFTTN GAMTIPVYDG
     KEVTDEEYDK LPEDVRNSFE EKTPILRQLM EKAMIKITEY DKKYREQLRN LEKYWALFTI
     SGIFEDLINE YSTNSDVIEF LNEIKNDIAE NFQDILSSDE SITNYYKKKY SVNVIIDNSS
     IKGAPVIEAN DPAYSSLIGK IEYFSHMGML KTDFTMIKPG LLHKANGGYL ILDAEKVMRS
     PYVWEALKNA LMNNEIKIEN LEGKMGLSVV HTLEPDPIPL NVKVILVGEE WMYEVLYQYD
     PDFKKLFNVK VAFDTEIELN KENAEYFAGF VKNIVKQHEL KDFTKGAVEE LLKYSCRINE
     RNDRFSAKFG VLKNIILEAN YISDRYSDTI PYVDKNAVIK AIQKHENMFS LYRDKIFDSI
     KDGQLIIDTE GEKIGQINGL TVVDFDTYSF GVPVKITGNV SSAKQVGVID IHRDADLSGK
     IHRKSTFIIE NYFYSKYNLD EHMVFSGSIS FEQTYSMLEG DSASLAEILV LLSAISKIPL
     KQYIAVTGSI DQHGNIQPVG GIIEKVEGFY YTCKLKGLKG NEGVIIPHQN IKNLVLNNEI
     EEDIKKGKFR IYAVKNVDEA IEIMTEYTAG KLNENGEFEE NSFNWHIIKR IKELRKIEDE
     KSHKKRFWLW GK
//
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