ID A0A075JGC9_9MICO Unreviewed; 365 AA.
AC A0A075JGC9;
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=HX89_04560 {ECO:0000313|EMBL:AIF40342.1};
OS Dermacoccus nishinomiyaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Dermacoccus.
OX NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF40342.1, ECO:0000313|Proteomes:UP000027986};
RN [1] {ECO:0000313|EMBL:AIF40342.1, ECO:0000313|Proteomes:UP000027986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M25 {ECO:0000313|EMBL:AIF40342.1,
RC ECO:0000313|Proteomes:UP000027986};
RA Hong K.W., Chan K.G.;
RT "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL Submitted (JUL-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}.
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DR EMBL; CP008889; AIF40342.1; -; Genomic_DNA.
DR RefSeq; WP_051805714.1; NZ_JAKREB010000013.1.
DR AlphaFoldDB; A0A075JGC9; -.
DR GeneID; 41840465; -.
DR KEGG; dni:HX89_04560; -.
DR eggNOG; COG3480; Bacteria.
DR HOGENOM; CLU_042037_1_0_11; -.
DR Proteomes; UP000027986; 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 CDD; cd00987; PDZ_serine_protease; 1.
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 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:UP000027986};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 252..353
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 365 AA; 38127 MW; 5EA6E4A40F4AB432 CRC64;
MSSRTVDAAE RRPSRWASMR TRTKVMLAIF VVVLLAVVAG FGIKVPYVIL RPGPAPNTLG
TFEGQKVLTL SGAKTYPTSG GLHFTTVSMV GGPGNRPSLI EYGLAKLDDH AQIYEESQLF
APQTTREQVQ QQNEAEMTGS QSSAEVVAAR QAGYDVPEMI EIAGISDSAS EAKKLLRVKD
VIVSVNGVKI ADSLSLQREM KKVTPGQKVQ LGITRGGKAM TFAVPTTKVE DRAVMGLALN
PKATMPFKVN ISVGDVGGPS AGTMFALAIY DELTPGALTG GKQIAGTGTM DSAGDVGAIG
GIREKVVGAR QAGATAFLAP ADNCAELKGH VPSGLDVYRV ATIKDAISTV EHVADGSTQG
LPRCG
//
