ID   A5N7E0_CLOK5            Unreviewed;       770 AA.
AC   A5N7E0;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   OrderedLocusNames=CKL_1179 {ECO:0000313|EMBL:EDK33221.1};
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK33221.1, ECO:0000313|Proteomes:UP000002411};
RN   [1] {ECO:0000313|EMBL:EDK33221.1, ECO:0000313|Proteomes:UP000002411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC   {ECO:0000313|Proteomes:UP000002411};
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK33221.1; -; Genomic_DNA.
DR   RefSeq; WP_012101560.1; NC_009706.1.
DR   AlphaFoldDB; A5N7E0; -.
DR   KEGG; ckl:CKL_1179; -.
DR   eggNOG; COG1067; Bacteria.
DR   HOGENOM; CLU_014785_1_1_9; -.
DR   Proteomes; UP000002411; 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; 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   ECO:0000313|EMBL:EDK33221.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000002411};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          555..750
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          138..165
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        645
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        688
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   770 AA;  88873 MW;  8E05AE7B383B3215 CRC64;
     MDRELSKEKI IYNFKLYDID FAHQDKHDIS KTFKFIPEYK EVYEKINMAL KINKEGYNIY
     LIDDFSRDKL ENIIEFIKST MENKNPLKDI CYVVVKDVKK PKVLFLTAGK GRELKVMLRK
     VQKKYFECTY EFYNGSSHRE KEILVEELQK ERSKLINKIL EISNKEGFTL KINENGFNFI
     PLKQNGEMMN ENEYEMLGMK EKENIIDKVN ILKNSSEEIL DKLKNIELDQ IEKIKFIINS
     YYEKETEDIK KEYLKLFKED NEALEFLNQA CSNIENEIKD IYSISYEDDK ENISRIIYRY
     SVNVLVDNSE NKEPPIIFEE DPNVNNLLGS VEYENINGTY TTGVNLIRPG SLLKANGGCL
     ILRVSSLLNN KSAYYYFKKS IISGKIDLNY DRGYLELLSL SGLKPEPIKF SEKIILIGDY
     NTYDLLYSYD EDFKKIFKIR VEYNALLNIN KETKISFLGK VFSICRSNKL HDVDEEGIKE
     LAKFLSRKAE DRDKLFMDDY ELERILMISD NRVIKDGRKI ITGTDIINTA YEEELIEKRM
     MDMYKGGQIF IDVTGKVVGQ INGLSVINTG YFNFGKPIKI TCTCLKGNGD VIDVQKESDL
     SGKIHNKAIN ILKGYIKRLT GGYDKCSVDF YLSFEQVYGQ IDGDSASVAE VISMISSLSK
     IGIRQNIAVT GSINQFGEIQ PIGGVNEKIE GFFKICKILG GTKGKGVLIP NSNIKSLALK
     NPVEKEVEKG NFHIYCMSNL KDAVEILMER DYNTVIHTAK RELKKYSSNR
//