ID K8E3G5_CARML Unreviewed; 306 AA.
AC K8E3G5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 2.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=BN424_1390 {ECO:0000313|EMBL:CCO10832.2};
OS Carnobacterium maltaromaticum LMA28.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO10832.2, ECO:0000313|Proteomes:UP000000212};
RN [1] {ECO:0000313|Proteomes:UP000000212}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL Genome Announc. 1:0-0(2013).
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; HE999757; CCO10832.2; -; Genomic_DNA.
DR AlphaFoldDB; K8E3G5; -.
DR STRING; 1234679.BN424_1390; -.
DR KEGG; cml:BN424_1390; -.
DR eggNOG; COG3480; Bacteria.
DR HOGENOM; CLU_042037_2_0_9; -.
DR Proteomes; UP000000212; Chromosome.
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; 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:UP000000212};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 190..306
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 241
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 306 AA; 33687 MW; 3006D5162964D6D9 CRC64;
MNELISVDNQ KDKEDGSFML TTVGVRQATA FTYFMRFLPF HEGLTKKELY GDVSSNKEFN
QVQDYYMTSS VNAAIELAYR TAGAEYKTHY KGVYVMSILD ESKFKGKLEV GDTIVSLDGH
SFKSSEEFID YVKSKKVGEE IDVVVNRNGS EKKVSAPLMK MDTDKKAGLG ISLVNDTTIT
TTIPVDVNTE EIGGPSAGLM FSLEIYTQLK GINLRDGRQI AGTGTISPDG TVGRIGGIDK
KVVAADKEGA TIFFAPDDEI DPAIKKKYPE LKTNYEEAKA AAKKIGTKMK IVPVKTFQDA
VDYLEK
//
