ID A0A081BGS5_9LACO Unreviewed; 347 AA.
AC A0A081BGS5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=LOSG293_030820 {ECO:0000313|EMBL:GAK47243.1};
OS Secundilactobacillus oryzae JCM 18671.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1291743 {ECO:0000313|EMBL:GAK47243.1, ECO:0000313|Proteomes:UP000028700};
RN [1] {ECO:0000313|EMBL:GAK47243.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG293 {ECO:0000313|EMBL:GAK47243.1};
RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Nakamura Y., Tohno M.;
RT "Draft Genome Sequence of Lactobacillus oryzae Strain SG293T.";
RL Genome Announc. 2:e00861-14(2014).
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:GAK47243.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BBJM01000003; GAK47243.1; -; Genomic_DNA.
DR RefSeq; WP_034526276.1; NZ_BBJM01000003.1.
DR AlphaFoldDB; A0A081BGS5; -.
DR STRING; 1291743.LOSG293_030820; -.
DR eggNOG; COG3480; Bacteria.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000028700; 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 CDD; cd00987; PDZ_serine_protease; 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.
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 Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 232..347
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 347 AA; 38172 MW; ACD1361CD3C8A232 CRC64;
MKNRKRRLTG TILALIAFVA ILIGLYWPMS SYIESPGSAD DLGSFVDISK HPDKDKGSFM
ITSVRIARAR PITYVWAKMH PDYYEVVSEA SVTGGQSGET YEKVQTFYMK SAINEAIATA
YKAAHQKIDK KYLGIYVLNI SKNSNFKSKL KVGDTVTKVN NQHFSSAYGF QSYIRKHKKN
DKLTIRFTHN GHQRQATGRL VNIGKGVAGI GITLTDNIKV TTKVPIQVDP GNIGGPSGGL
MFSLQIYSQL TGDNITHGQK IAGTGTINPD GSVGEIGGID KKIIAAKKAG ATIFFAPYVK
PTKELLKYEP NHLTNYQQAK KTAKKYAPNM KIVPVKSFDQ ALAYLQK
//
