ID   D8GQJ5_CLOLD            Unreviewed;       773 AA.
AC   D8GQJ5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   OrderedLocusNames=CLJU_c10500 {ECO:0000313|EMBL:ADK14118.1};
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK14118.1, ECO:0000313|Proteomes:UP000001656};
RN   [1] {ECO:0000313|EMBL:ADK14118.1, ECO:0000313|Proteomes:UP000001656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55383 / DSM 13528 / PETC
RC   {ECO:0000313|Proteomes:UP000001656};
RX   PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA   Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA   Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT   "Clostridium ljungdahlii represents a microbial production platform based
RT   on syngas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
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; CP001666; ADK14118.1; -; Genomic_DNA.
DR   RefSeq; WP_013237715.1; NZ_LITS01000015.1.
DR   AlphaFoldDB; D8GQJ5; -.
DR   STRING; 748727.CLJU_c10500; -.
DR   KEGG; clj:CLJU_c10500; -.
DR   PATRIC; fig|748727.19.peg.4323; -.
DR   eggNOG; COG1067; Bacteria.
DR   HOGENOM; CLU_014785_0_1_9; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000001656; 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   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW   ECO:0000313|EMBL:ADK14118.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          556..751
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        646
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        689
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   773 AA;  89377 MW;  430F926E2705C5E5 CRC64;
     MNYRELPKDQ IIYDFKLDDI DFSEDDRDDL NRNVNYMPEY SRVYENMRDA LTIDKQGYNV
     YLIDEFSKDK LKNIKKFINE TMKDKIELQD ICYIVMKDIK NPKVLFLRSG KGKKLKNMLK
     KIQNIYANST YEFYNGYEDK QKKLLVQNIQ KKRSYLINKI VEMSKNEGFS LKITESGFSF
     VPLKENGKMM NEIEYESLDL EKKEQMVNKV NTLKIHAERI LDKLKDMESY EMEKIKILID
     EHYKKDTKKL KEEYFNVFSK DNKALEFLSN ICNNIESEIK EIYSINYEDD VDNIRNIIYR
     YSVNVLVDNS DNDKLPIVFE EDPSINNLLG SIEYENKNGT YVTDPSLIRP GSLLKANGGI
     LVLRVSSLLS NKGAYYYLKK SIISGKVDLN YNRGYLELLS LSGLKPEPIE FNEKIILIGD
     YHTYDLLYTY DEDFKKIFRI RAESKSILQM DRDAKKAFLY KVLSICKNNK LHPADEGAVK
     ELAKFLSRKA ENRDKLFMDD YDLERILIIS DKRVCEDHRD FINEEDITNT AYKEEIIEGQ
     VVDSYTEGQI FIDVKGKTVG QVNALSIIDT GYFNFGKPIR ITCSCYKGNG NIIDIQKESD
     LSGKIHNKAI NILKGHVKNL SGGYNRVPVD FYLSFEQIYG RVDGDSASVA ELVSIISALT
     KISIKQNIAV TGSINQFGEI QPIGGVNEKI EGFFKICKVL DTTKGKGVLI PKSNASSLAL
     KSEVEKEITD GNFHIYIMSN LKDAVEILMG ENYDNVIHEA RKELKKYYKN KEQ
//