ID A0A1M4VX74_9LACT Unreviewed; 367 AA.
AC A0A1M4VX74;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=SAMN02745249_01036 {ECO:0000313|EMBL:SHE73558.1};
OS Atopostipes suicloacalis DSM 15692.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Atopostipes.
OX NCBI_TaxID=1121025 {ECO:0000313|EMBL:SHE73558.1, ECO:0000313|Proteomes:UP000184128};
RN [1] {ECO:0000313|EMBL:SHE73558.1, ECO:0000313|Proteomes:UP000184128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15692 {ECO:0000313|EMBL:SHE73558.1,
RC ECO:0000313|Proteomes:UP000184128};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQUF01000013; SHE73558.1; -; Genomic_DNA.
DR RefSeq; WP_073297358.1; NZ_FQUF01000013.1.
DR AlphaFoldDB; A0A1M4VX74; -.
DR STRING; 1121025.SAMN02745249_01036; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000184128; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Reference proteome {ECO:0000313|Proteomes:UP000184128};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 227..343
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 367 AA; 40246 MW; 011C52EB63DCE1EF CRC64;
MKKLSKWIKA LLILGVLYLF FFLPLPLYLE VPGRAFELND MVEVDDEYFT DSGEFYITTV
GIQQATPFTA LSSVLPFRDL VTEKDLFGDI DNYEEYDVIQ QYYMDSSINT AIQVAFEAAD
KDYELHYNGV YVLQVLDNSS FAGELKVGDT VKSVDGHSFN NSHDFIEYVA DKDVGEKVDI
EFEREGQLLT AFGELVPLDT GIAGIGIGLV DNTSIETVPA VSIHSGEIGG PSAGLMFSLQ
IYSQLTGENI HGSHKIAGTG TISPDGSVGR IGGIAKKVVA ADEEGAEYFF APDDELDEDV
RKLYPELQSN YQEALDAAEA IDTDMEIIPV KTITDALDFL KELKQETIAL SIQPSLGNIG
DWVPAAD
//
