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Database: UniProt
Entry: D8F4L6_9DELT
LinkDB: D8F4L6_9DELT
Original site: D8F4L6_9DELT 
ID   D8F4L6_9DELT            Unreviewed;       827 AA.
AC   D8F4L6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=NPH_3406 {ECO:0000313|EMBL:EFK09303.1};
OS   delta proteobacterium NaphS2.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK09303.1, ECO:0000313|Proteomes:UP000003834};
RN   [1] {ECO:0000313|EMBL:EFK09303.1, ECO:0000313|Proteomes:UP000003834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NaphS2 {ECO:0000313|EMBL:EFK09303.1,
RC   ECO:0000313|Proteomes:UP000003834};
RX   PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA   Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA   Lipton M.S., Deboy R., Methe B.A.;
RT   "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT   Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL   PLoS ONE 5:E14072-E14072(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}.
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:EFK09303.1}.
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DR   EMBL; ADZZ01000305; EFK09303.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8F4L6; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000003834; 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; IPR046844; Lon-like_helical.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR046843; LonB_AAA-LID.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002885; Pentatricopeptide_rpt.
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   Pfam; PF20436; LonB_AAA-LID; 1.
DR   Pfam; PF20437; LonC_helical; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR   PROSITE; PS51375; PPR; 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:UP000003834};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          578..773
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          222..256
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        668
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        711
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   827 AA;  93076 MW;  BC0320C74FADD757 CRC64;
     MPKKTSHKEV PTDKLRWRLD PATLPFKSTD DLEPLDEIVG QKRAVEAFRF GLGIESHGYN
     VFVTGLAGTG RMSTVRKLLE EMSRNERVPD DLCYINNFKN TEAPILLRLK GGEGAAFKKD
     IHDFVELLKK QIPMLFESQE YINTKKELMA AYEARGKSFF KNLDEKVKEE GFTLVDVQVG
     QIKRPEVMPL VDGNPIHIDQ VEAMVEKGRF PKDEFEQMKE KHGKLRERVE QIFIELRDLQ
     KEVQEKIEEM DRLTFLNNAS DMAKPLTEKY DHPKIQAYLK AMLEDMGENL QIFNPQQQQA
     QVPGLMIPMA SEGDRFQPYQ INLLVDNSEQ KSSPVIVEDY PTYRNIFGSI ERIVDRAGVW
     RTDFSKIKAG SLLKAQGGYL VINLMDAIVE PGVWQALKRA LKSEKLEIQT YDPFYLFTTS
     GLKPEPIDLD IKVVVVADAY LYHLLLFYDP DMSKVFKVRA DFDTAMDKNE ESIVQISRFI
     KMKGDEEKLK PFDRTAVAVL VEQAVRMTGR QEKISTSFPQ LTDYLREASY LADQEKEKIV
     RDHHVEKVLE SRKFRSGMVE EHIQEMIDRG TLMIDVAGEA VGQVNGLAVY SMGDYAFGKP
     SRITCSTAMG RAGIINIERE ADLSGSTHNK GVLILGGYLR KKYAQDKPLT MSASIAFEQS
     YGGVDGDSAS STEIYALLSS LSEVPIKQYI AVTGSVNQNG QVQAIGGVNE KIEGFFDCCR
     KKGADKSQGV MIPESNVKDL MLRQDVVNAV KDGKFHIYPV STIDEGIEIL TGKKAGKRKA
     DGTYTKGSIN QLVDDKLKSL AEGLKNFAGD KEEGNKESKK KGCAQCS
//
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