ID   C4IDI0_CLOBU            Unreviewed;       771 AA.
AC   C4IDI0;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=CLP_3410 {ECO:0000313|EMBL:EEP55327.1};
OS   Clostridium butyricum E4 str. BoNT E BL5262.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP55327.1, ECO:0000313|Proteomes:UP000003081};
RN   [1] {ECO:0000313|EMBL:EEP55327.1, ECO:0000313|Proteomes:UP000003081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA   Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA   Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.;
RL   Submitted (AUG-2009) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEP55327.1}.
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DR   EMBL; ACOM01000004; EEP55327.1; -; Genomic_DNA.
DR   RefSeq; WP_002581969.1; NZ_ACOM01000004.1.
DR   AlphaFoldDB; C4IDI0; -.
DR   STRING; 1492.ATN24_05130; -.
DR   GeneID; 66382588; -.
DR   eggNOG; COG1067; Bacteria.
DR   HOGENOM; CLU_014785_0_1_9; -.
DR   Proteomes; UP000003081; Unassembled WGS sequence.
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:UP000003081};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          547..742
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          194..221
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        637
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        680
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   771 AA;  88025 MW;  1845F5A58146FD91 CRC64;
     MKRELTPSEI IFSASVNDVA KQTNINRIPR SNTTLNKIKK ALSIQKDGYN IYYVDSFSKE
     KLEELVEFIE NMYIDDKEPK DICYVSNNDS SNPIVLVLEN GKGQLLKEMI EDMKEKYLEC
     INEFYNTSSD DEKEDIIDDV TEKRSNYITN LMDMAKAKNF EIKATTGGFV FIPIKEEGDE
     MTKDEYDDLE DEDQESIEKQ ATNLKKEAEV ILEKLKEIEI DSIEKLKSLY RDHIKNKMQS
     YKDDFLLEFI AYDNVYRYLI EMFEYLDDEI VECYTINLED DEEYIQEVLG KFSVNVLVDN
     TGVNHPRVIY EEDPTVSNLI GNIEYRNTTG GYSTDMSLIS AGSLVKANGG CLILRLTSLI
     NSGSSYYYLK KALIHGQVDY NYTKSYLEVL SIAGLKPQPI PINVKVILIG DYESYEVLFD
     KDEDFKMIFP IRIEAESELN YDINIRKNIC NIIKKKIIKD NLLSMTDEAM DELMKYLARI
     AGSRSKISID EYYVNKILYL ADNNAKLENK NEIDRQDIIN IAYEEEKILR DVMESYTNKK
     ILITTTGEKV GIINALSVVG TGSYNFGKPM RVTCLALQGD GNIIDIHKEC KMSGQIHEKS
     ISILRGLLSS LISPYEKLPV DLQLSFEQTY GMIEGDSASV AEIICVLSAL SKKPIKQNIA
     VTGSINQFGE IQPIGGVNEK IEGFHRVCKL IDTVENKGVL IPSSNTDELI LNAEVEEDIR
     NGRFHIYTMD SLDDAIEVLI LKEGETVTDF FKSLNDEIVK YKYDKGSKKK K
//