ID A0A081NY40_9BACL Unreviewed; 357 AA.
AC A0A081NY40;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=ET33_17205 {ECO:0000313|EMBL:KEQ23363.1};
OS Paenibacillus tyrfis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ23363.1, ECO:0000313|Proteomes:UP000028123};
RN [1] {ECO:0000313|EMBL:KEQ23363.1, ECO:0000313|Proteomes:UP000028123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ23363.1,
RC ECO:0000313|Proteomes:UP000028123};
RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT "Draft genome sequence of Paenibacillus sp. MSt1.";
RL Submitted (JUN-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 -!- 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:KEQ23363.1}.
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DR EMBL; JNVM01000023; KEQ23363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A081NY40; -.
DR eggNOG; COG3480; Bacteria.
DR Proteomes; UP000028123; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.30.42.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; NF041438; SepM_fam_S16; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF48; ENDOPEPTIDASE LA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Reference proteome {ECO:0000313|Proteomes:UP000028123};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..187
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 238..351
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 357 AA; 38675 MW; 808E25149B8A3850 CRC64;
MKRASRVVFS VFIAIALLYV VYFMPLPLYI FKPGTAENIH PMVHVKQAAV EKGKFMLTTV
QVADATVFGY LLSYVRPYEE LRLKRDLLRN NETEAEYSQR QEVVMLTSQA DAIQAVYNRL
KIPYHISKDG VVIQQVYPDV PAHEVLQAGD TIVKIGDKPI QTMDEVRGGV TGKKAGDSVS
ISYKRKGVIR TKDIALAALP TDPSAQPAEA SRVGLGVVLS ELHSVKADSE EQQVTIKAGD
IGGPSAGLMF SLEIYNQLTP GDITKGYKVA GTGEIDPEGH VGVIGGIQHK IVAADRAGAE
IFFSPADYKA PNGQTIPNYS DAKKRADELG TKMTVVPVAT MAEALDYLAK LPVKTGS
//
