ID B9MJV9_CALBD Unreviewed; 787 AA.
AC B9MJV9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=Athe_1519 {ECO:0000313|EMBL:ACM60617.1};
OS Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / KCTC 15123 /
OS Z-1320) (Anaerocellum thermophilum).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=521460 {ECO:0000313|EMBL:ACM60617.1, ECO:0000313|Proteomes:UP000007723};
RN [1] {ECO:0000313|Proteomes:UP000007723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320
RC {ECO:0000313|Proteomes:UP000007723};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kataeva I., Adams M.W.W.;
RT "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL Submitted (JAN-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}.
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DR EMBL; CP001393; ACM60617.1; -; Genomic_DNA.
DR RefSeq; WP_015907970.1; NC_012034.1.
DR AlphaFoldDB; B9MJV9; -.
DR STRING; 521460.Athe_1519; -.
DR GeneID; 31772869; -.
DR KEGG; ate:Athe_1519; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_0_1_9; -.
DR Proteomes; UP000007723; 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; 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; 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; 2.
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}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 563..758
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 131..162
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 198..243
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 653
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 696
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 787 AA; 90279 MW; 6756894374929F19 CRC64;
MKLTPDKLKK NVDLSNFEFK TTNEIEPLTT IIGQERAKRA FEFGLSVTTK GYNIYMCGPT
GTGKTSFAEN YLKEIAKNKP APNDWVYVYN FANHDSPIAI SLPKGMGKVF RKDMTDFLEF
VINDLKKVFN SEEYENDKNN IYNEYQEKRT QLLDKLAEEA REYDFEIKYT PSGVYFIPIV
NGRAISEEEY PELEKTIRDE IEKKVKKLQL ETQEVLKKIK VLEKELKERI KELQKRIAVF
TISHYVYEIR SKYKDNIKIL DYIDSVTDDI IENLDDFLDK EEEDTQIPLQ FVPYKKFSRL
DKYKVNVIVD NSELDGAPVV YEVNPTYYNL IGKIEYDNEM GNILVTDYTR IKAGAIHKAN
GGYLILQAKD LLSYPQAWEA LKRVLKTGQI YIENLKDIYG LFITPSLKPE PIPVDLKVIL
IGSEYIYNIL YTYDEDFKKL FKIKADFDSE MDYNQDNLYK MIQFISSFCK KENALPFSKD
AVEKVIEYSC RLVENQEKLS TRFNEIVEIL AEANTWAQLE RSNVVRKEHV SKAICEKEYR
SAKYEEKINQ MIEEGTILVD VDGYKVGQIN ALAILDVGDY VFGKPSLITV TTSSGRSGII
NIEREVQMSG KTHSKGILII SGYISQLFAQ DMPLTLNATI CFEQLYSGIE GDSASAAELC
ALLSALSDMP IYQGIAITGS VNQKGVIQPV GGVTKKIEGF YYVCKKKGLN GKQGVIIPHQ
NIKNLVLCDE VVEEVRKENF HIWAVKTIDE AIEILTGKKF DEVVLLARQK LKRYLDNLVS
FSDKKDE
//
