ID Q8XKK3_CLOPE Unreviewed; 570 AA.
AC Q8XKK3;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN Name=lonB {ECO:0000313|EMBL:BAB81097.1};
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81097.1, ECO:0000313|Proteomes:UP000000818};
RN [1] {ECO:0000313|EMBL:BAB81097.1, ECO:0000313|Proteomes:UP000000818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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 -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|ARBA:ARBA00026070}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; BA000016; BAB81097.1; -; Genomic_DNA.
DR RefSeq; WP_011010424.1; NC_003366.1.
DR AlphaFoldDB; Q8XKK3; -.
DR STRING; 195102.gene:10490655; -.
DR MEROPS; S16.005; -.
DR KEGG; cpe:CPE1391; -.
DR HOGENOM; CLU_020014_0_0_9; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
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; IPR014251; Spore_LonB.
DR NCBIfam; TIGR02902; spore_lonB; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF64; LON PROTEASE; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF01078; Mg_chelatase; 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; 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|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..265
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 349..537
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 490
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 570 AA; 62515 MW; E5527A3ABBD85509 CRC64;
MNTYTFIMFL QLLMSILFYI YMSKSFASKK KDNSVLEKEN EKEMEKLNKL RMIKLTEPLT
EKSRPSNLEE IIGQEKGIKA LKAALCGPNP QHVIIYGPPG VGKTAAARII LEEAKKMAAS
PFNKDSKFVE IDATTLRFDE RGIADPLIGS VHDPIYQGAG SLGIAGVPQP KPGAVTKAHG
GILFIDEIGE LHPIELNKLL KVLEDRKVFL DSAYYSSEDP NTPRYIKEIF DNGLPADFRL
IGATTRSPEE IVPAIRSRCV EIFFRGLTVE EIRKIALNAT NKVGYRISDE GLDIVSRYCT
NGREVINLVQ LCSGLAINEN RDYIKESDIY WVIENGQYNP RMERMINDKP EIGYVNGLAV
YGANNGALME IEATAKLSSN SIGSIKITGI VDDEELGGGE KKIKRKSTAY CSVQNVLTVL
DNIFNLNSKA YDIHVNFPGG IPVDGPSAGI SIATAIYSAI KGVPVNNRVA MTGEISIKGK
VKPIGGVNAK ILAAKRAGVE LVIVPKENLS SITRDIDGIK IVGVKKIEEV LDLALYEEEC
IEKESLIIKD NRAFFGTGAL NAESIKKANT
//
