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Database: UniProt
Entry: A0A0E4HE72_9BACL
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ID   A0A0E4HE72_9BACL        Unreviewed;       569 AA.
AC   A0A0E4HE72;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   Name=lon2 {ECO:0000313|EMBL:CQR57862.1};
GN   ORFNames=PRIO_5473 {ECO:0000313|EMBL:CQR57862.1};
OS   Paenibacillus riograndensis SBR5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC   Paenibacillus sonchi group.
OX   NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR57862.1, ECO:0000313|Proteomes:UP000033163};
RN   [1] {ECO:0000313|Proteomes:UP000033163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg D.;
RL   Submitted (MAR-2015) 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   -!- 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; LN831776; CQR57862.1; -; Genomic_DNA.
DR   RefSeq; WP_046505542.1; NZ_LN831776.1.
DR   AlphaFoldDB; A0A0E4HE72; -.
DR   STRING; 483937.AMQ84_18635; -.
DR   KEGG; pri:PRIO_5473; -.
DR   PATRIC; fig|1073571.4.peg.5865; -.
DR   HOGENOM; CLU_020014_0_0_9; -.
DR   Proteomes; UP000033163; Chromosome I.
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; 2.
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; 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; 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; 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|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};
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..26
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..536
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        489
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   569 AA;  60896 MW;  38426B01C59CC9AC CRC64;
     MELSILLMIV QLFFALVIGV YFWNLLRGQK TNKTAVDRES RKELDKLRKM RMISLTKPLS
     EKTRPASIGD IVGQKDGLRA LKAALCSANP QHVIIYGPPG VGKTAAARVV MEEAKKNGLS
     PFKSDAKFTE IDATTARFDE RGIADPLIGS VHDPIYQGAG AMGVAGVPQP KPGAVTKAHG
     GILFLDEIGE LHPIQMNKLL KVLEDRKVLL ESAYYNSEDS NTPAYIHDIF QNGLPADFRL
     VGATTRSPEE ISPALRSRCM EIYFRPLLPE EIAVIGRDAV QKIGLKPSPE AIEVVQQYAT
     NGREAVNMIQ LAAGLALTEG RDTLSAAEVE WVASSSQLPM RTERKIPSSP QIGLVNGLAV
     YGPGMGTLLE IEVSAAPAKS GQGRLNVTGV VDEEETRGGS RTIRRKSMAK GSLENVLTVL
     RAMNLEPDRY DLHVNFPGGT PIDGPSAGVA MAVAIVSAIR HLPVDNTVAI TGEIGIHGRV
     KPVGGVIAKV EAAFQAGATT VLIPKENWQS LFADLAPLQV IPMETVEEVF RHLFGAETAD
     VRLPAVSGET FSAAPSLLKA DASGDSATG
//
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