ID   A0A1D7XIF3_9CLOT        Unreviewed;       769 AA.
AC   A0A1D7XIF3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=BGI42_04170 {ECO:0000313|EMBL:AOR22960.1};
OS   Clostridium taeniosporum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=394958 {ECO:0000313|EMBL:AOR22960.1, ECO:0000313|Proteomes:UP000094652};
RN   [1] {ECO:0000313|Proteomes:UP000094652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1/k {ECO:0000313|Proteomes:UP000094652};
RA   Walker J.R.;
RT   "Genomics of Clostridium taeniosporum, an organism which forms endospores
RT   with ribbon-like appendages.";
RL   Submitted (SEP-2016) 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; CP017253; AOR22960.1; -; Genomic_DNA.
DR   RefSeq; WP_069679116.1; NZ_CP017253.2.
DR   AlphaFoldDB; A0A1D7XIF3; -.
DR   STRING; 394958.BGI42_04170; -.
DR   KEGG; ctae:BGI42_04170; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000094652; 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; 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   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000094652};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          548..743
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          179..221
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        638
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        681
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   769 AA;  87532 MW;  FC49206E8D3E511D CRC64;
     MKNELTPSEV IFKCSFKELS DKERLAELPE VTSRLKDIKR ALKIKKNGYN LYYIDSFAMD
     KLSSLMDYVS EIYQEEGAPK DICYVTTDDL LNPKVLFLPS GKGTLLKERI DDIKNQYFDC
     VIEFYNGSSN EEKEELIEQT KEKRNKYISD LMKRAKENNF DVKATNGGFV FIPLKSEGNE
     MTEDEYDELE NDEQGVINEQ VSELKKEAQL VLNKLTALEI KSINDLRVMY GEYLKKEMKE
     AKEDLLFEFV TDKLACMHLS QMFDWIEDQL VECYTVSLEE DQSYIDEIFI KFQINVLVDN
     KDVPHPRVIF EENPTINNLI GNIEYKNSNG GYLPDIGLIH PGSLLRANEG CLILNLNSLL
     AGGYSYYYLK KVLMFGKVDY SYTKNYLEVL SLEGLKPESI PVNVKVILIG DYEAFSILYE
     KDEEFKRIFP LKVEMESELK CNDASRSLIA NYIKNKAKNE GLLDLEQGAI EEIFKYLSRI
     IGNRNKISID NYYIDKILYL ANDKANNDGR FSIIRDDIIS SYHCDDKDIN EQMLESYKNN
     KILLSINGEK VGSTNGLAVI GTSLFSLGRP MRITCLAFQG TGKIIDVHKE SKLSGNIHEK
     SIGILTGLIN NLLSPYESLP VDFQLSFEQT YSLVEGDSAS VAEIICILSA LSKKPIKQNI
     AVTGSINQFG EVQPIGMVNE KIEGFYTVCS AMDTVSGKGV LIPNMNKDEL ILDKDVEESI
     SKGDFHIYTM STIEDAIEIL ILNDGETIKG FFKIIEEEIA KYKPSKRKK
//