ID A5IL73_THEP1 Unreviewed; 794 AA.
AC A5IL73;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=Tpet_0928 {ECO:0000313|EMBL:ABQ46946.1};
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=390874 {ECO:0000313|EMBL:ABQ46946.1, ECO:0000313|Proteomes:UP000006558};
RN [1] {ECO:0000313|Proteomes:UP000006558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1
RC {ECO:0000313|Proteomes:UP000006558};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABQ46946.1, ECO:0000313|Proteomes:UP000006558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1
RC {ECO:0000313|Proteomes:UP000006558};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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; CP000702; ABQ46946.1; -; Genomic_DNA.
DR RefSeq; WP_004082420.1; NC_009486.1.
DR AlphaFoldDB; A5IL73; -.
DR STRING; 390874.Tpet_0928; -.
DR KEGG; tpt:Tpet_0928; -.
DR eggNOG; COG0433; Bacteria.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_0_1_0; -.
DR Proteomes; UP000006558; 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}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 552..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 794 AA; 90264 MW; F21813702E589E05 CRC64;
MIRKLRPDEI NSFDLDFLNF QTTEEVPPNE GFIGQKRAKE AIETGIRIRE KGYNIFVTGM
TGTGRRTFVQ MMLQDVAKKL PVPNDWGYVY NFENPYEPKA ISFKAGQGRR FKKRLEDLIN
EVVEALNKSF ESEEFARKIS EMEEKYALMR KQLWESLEAK ASELGFVVQL TPAGVVMLPV
VDGKPLPPEA VNALPDQAIR EIEERQMKLK HLVDGTLYRI RKLDIEFRKS LEEFHKRTAL
FAIDPLFVEV ESEFENEGVK EFLESVKKDI VENLLDFLRM DARERKEIYM RKYSLNLIVD
NSDLTGAPVI YETNPTYSNL FGKIEYYVRG GFLHTDFSMI RPGSVHKANG GFLIVEAERL
LSQPYAWYNL KRVLMESQIS VENLEHTLGV SSTITLKPEK IPLDLKVVII GTPYLYELLY
ELDPDFRKLF RIKAEFDWEI PRNELNVQKY VSFISSVCRE KNLPHFDRGA VKRVIWYAMR
NAGNSTKLSA VFGDIVNLIV ESGELARLEG SEVTTSDHVL KAYQAMENRR NLLEEKYDEM
IKTFDLMIEV TGSKVGQING LTVLDLGDHS FGVPVKITAK VYLGRPGVVD IQREADLSGK
IHSKAVLILE GFLGSRYAQD FPLSVSASIS FEQVYSEVEG DSASLAEALA LLSAISKVPI
KQGIAVTGSI NQHGEVQPVG GIVEKVEGFY RACKTRGFDG EQGVIIPKAN AKNLVLKDEI
IQAMKKGLFH IWTVETIDDA IEIVMGMKAG RVTKTGKFER NSVNYLVYRE LKKMKKLLDG
VPEERKKKKR KGKK
//
