ID   Q894A7_CLOTE            Unreviewed;       762 AA.
AC   Q894A7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   OrderedLocusNames=CTC_01644 {ECO:0000313|EMBL:AAO36185.1};
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36185.1, ECO:0000313|Proteomes:UP000001412};
RN   [1] {ECO:0000313|EMBL:AAO36185.1, ECO:0000313|Proteomes:UP000001412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA   Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO36185.1; -; Genomic_DNA.
DR   RefSeq; WP_011099845.1; NC_004557.1.
DR   AlphaFoldDB; Q894A7; -.
DR   STRING; 212717.CTC_01644; -.
DR   GeneID; 24254429; -.
DR   KEGG; ctc:CTC_01644; -.
DR   HOGENOM; CLU_014785_1_1_9; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000001412; 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; 1.
DR   InterPro; IPR041699; AAA_32.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
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   PRINTS; PR00830; ENDOLAPTASE.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW   ECO:0000313|EMBL:AAO36185.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000001412};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          544..739
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          123..154
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        634
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        677
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   762 AA;  88175 MW;  D943B865A42F75F1 CRC64;
     MEGFRLNKIK YEIDFNDVDF QEEDCIAEYY ETYKEIKKAL SIDKEGYNLY LIDDFSKDKL
     KNIIYFINKE FKNVNLEDIC YVIKENIKKP TPIILSWGNG IILKKALKDI QDKYWNLASE
     FYNSSKNEKK EQFLEEIEDM KSDLLEKIIE TSKDKGFDIK LSKSGIVFEP LKEDGEPMTE
     KEFELLSREK RGKILVKISE LKKEAEHLLE VLHDKEEKLL EGIKKIFKEY LNENMKDIKA
     YYDNLLKEER QATEYLNYVY SKIEMDLVES YSEDYDFEEE DTAEIIYKYG VSIILDNKDT
     ECMPCIYEED PNLENLLGAI EYENKNGNYV TDINMIKPGS MLRANGGCLI LRANKLLTNA
     ASYYYFKKTI MSGKIDMNYS KGYLEVLALS GMQPEPIKIK EKVILIGDFE TYDILYNHDE
     DFRKIFKIRG QYDPIVNINK KSKSSLISSI DDICKKNNLK PVKEGGIFEI AKALSRKAED
     RRKFYFKLEE LEKILVMANN RAVEENKDFI DGEEVVSGFY KEDMLEDKII EEFKDGKIYM
     NLKGNAIGEI NGLTVLDAGY LSFGKPVKIT CNCYNGSGNI IDVQKDSNLS GKIHNKAINI
     LKGYINDTFG RYSRLPVDFH ISFEQVYGKI DGDSASVAEV ISIISAISRI GIKRNIAVTG
     SINQKGEVQP IGGVNEKIEG FFNVCKNLDT VKNKGVAIPY SNRDNLVLNR EVEEEVENGN
     FRIYLMKTVE DAVEIFMCNE KVTCKDVFEE ANRELKKYYR RK
//