ID B1V5T0_CLOPF Unreviewed; 632 AA.
AC B1V5T0;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=CJD_3291 {ECO:0000313|EMBL:EDT70851.1};
OS Clostridium perfringens D str. JGS1721.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=488537 {ECO:0000313|EMBL:EDT70851.1, ECO:0000313|Proteomes:UP000003188};
RN [1] {ECO:0000313|EMBL:EDT70851.1, ECO:0000313|Proteomes:UP000003188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D str. JGS1721 {ECO:0000313|Proteomes:UP000003188};
RA Paulsen I., Sebastian Y.;
RL Submitted (MAR-2008) 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:EDT70851.1}.
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DR EMBL; ABOO01000036; EDT70851.1; -; Genomic_DNA.
DR RefSeq; WP_003459992.1; NZ_ABOO01000036.1.
DR AlphaFoldDB; B1V5T0; -.
DR MEROPS; S16.005; -.
DR Proteomes; UP000003188; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR014252; Spore_LonC.
DR NCBIfam; TIGR02903; spore_lon_C; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF64; LON PROTEASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
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; PS01046; LON_SER; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 179..351
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 459..632
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 543
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 586
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 632 AA; 70258 MW; 96119090D6F91FA3 CRC64;
MKSIKELEVL QDVMNSELGV ESQVEALKDI INNILDEGAF RARVIRFKVQ NYINSTDPYE
RLYGLSKIVS EGKGLSEVPT EETINEALED VCAMISDAIA RRYVQNKIEK EVEQFLMEKQ
EKYVDELRVN IMKKKKGPEN AKTEKKLEEL EELDERVPNK NIMSLLRPDS FDEVVGQERA
VKSLLSKLAS PYPQHIILYG PPGVGKTTAA RIALETAKKL KSTPFDDRSK FIEVNGTTLR
WDPREITNPL LGSVHDPIYQ GSKRDLAEIG VPEPKPGLVT EAHGGILFID EIGELDEILQ
NKLLKVLEDK RVEFSSSYYD PDDENTPKYI KYLFDKGAPA DFVLIGATTR EPGEINPALR
SRCTEVYFEP LSSRDIEKIV LNAAKKLNVK LEEGLEKKIA SYTIEGRRAV NILADAYGHA
IYGLEGEVPE DLEITSKDLN EVVSIGRFTP YEILENLEEK EVGHVYGLGV SGFLGSTIEI
EATAFKAKKK GAGKIRFNDT AGSMAKDSVF NAASVIKRLT DKDINDYDIH VNVIGGGKID
GPSAGAAITI CIMSALLEKP IRQDLAITGE ISLRGKIKPV GGIFEKIYGA RRKGIKLVTV
PKDNENEIPK GLEDIEVKAI SSIEELMEIA FN
//
