ID A0A089K6A7_9BACL Unreviewed; 569 AA.
AC A0A089K6A7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=R50912_27400 {ECO:0000313|EMBL:AIQ43330.1};
OS Paenibacillus sp. FSL R5-0912.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536771 {ECO:0000313|EMBL:AIQ43330.1, ECO:0000313|Proteomes:UP000029512};
RN [1] {ECO:0000313|EMBL:AIQ43330.1, ECO:0000313|Proteomes:UP000029512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0912 {ECO:0000313|EMBL:AIQ43330.1,
RC ECO:0000313|Proteomes:UP000029512};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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; CP009282; AIQ43330.1; -; Genomic_DNA.
DR RefSeq; WP_042238998.1; NZ_CP009282.1.
DR AlphaFoldDB; A0A089K6A7; -.
DR KEGG; paeq:R50912_27400; -.
DR HOGENOM; CLU_020014_0_0_9; -.
DR Proteomes; UP000029512; Chromosome.
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; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000029512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
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; 61159 MW; 8E85BC78124D0452 CRC64;
MQLSILLMIV QLFFALVIGV YFWNLLRGQK TNKTAVDRES RKELDKLRKM RMISLTKPLS
EKTRPASIDD IVGQKDGLRA LKAALCSANP QHVIIYGPPG VGKTAAARVV MEEAKKNALS
PFKREAKFTE IDATTARFDE RGIADPLIGS VHDPIYQGAG AMGVAGVPQP KPGAVTKAHG
GILFLDEIGE LHPIQMNKLL KVLEDRKVLL ESAYYNSEDS NTPAYIHDIF QNGLPADFRL
VGATTRSPDE ISPALRSRCM EIYFRPLLPE EIAVIGRDAV QKIGLKPSPE AVEVVQQYAT
NGREAVNMIQ LAAGLALTEG RDTLSAAEVE WVASSSQLPL RTERKIPTSP QIGLVNGLAV
YGPGMGTLLE IEVSAAPAAH GQGRLNITGV VDEEELRGGS RTTRRKSMAR GSIENVLTVL
RTMKLEPDHY DLHINFPGGT PIDGPSAGVA MAVAIVSAIR QLPVDNTVAI TGEIGIHGRV
KPVGGVVAKV EAAFQAGATT VLIPKENWQS LFADLGPLRV IPMDTVEEVF RHLFGADTAD
VRMPAVSGET FSSAPSLLKA DASGESMPG
//