ID A0A1H1CGQ9_9BACI Unreviewed; 340 AA.
AC A0A1H1CGQ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=SAMN05216231_2245 {ECO:0000313|EMBL:SDQ63381.1};
OS Virgibacillus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=553311 {ECO:0000313|EMBL:SDQ63381.1, ECO:0000313|Proteomes:UP000199444};
RN [1] {ECO:0000313|EMBL:SDQ63381.1, ECO:0000313|Proteomes:UP000199444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10449 {ECO:0000313|EMBL:SDQ63381.1,
RC ECO:0000313|Proteomes:UP000199444};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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; FNKD01000002; SDQ63381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1CGQ9; -.
DR STRING; 553311.SAMN05216231_2245; -.
DR Proteomes; UP000199444; 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; 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 SMART; SM00228; PDZ; 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:UP000199444};
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 101..187
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 227..337
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 280
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 340 AA; 37502 MW; AAEB2FC07C927DF1 CRC64;
MNFTKKHIIY LIVVIAIAFF LSTYQLPYYV YKPGGADALN PIVNVEGGYD SKGDMHLVTV
RGGQATPVQY LWAKVLPNHE IYPLSEVRPE GVSENEYFHA QLQMMESSQE ASTVVAYKAA
DEDITINYEG VYVVAVVNGM PADGKLESGD RITEIDGNEI KESKDLINYV ENKQAGDTIN
LEVERGEKQL TKEVQLERFK EADNKVGIGI RLVTDRSVKV DPKVNFSSGS IGGPSAGLMF
SLEIYDQLTE NDLTKGNQIA GTGEVDYNGN VLRIGGIDKK VIAADQEDCD IFFAPNDNGA
EGSNYEVAKK TAEEIDTDMK IVPVDTFEDA LNYLQNIESE
//
