ID A0A1M6G6P6_9CLOT Unreviewed; 370 AA.
AC A0A1M6G6P6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=SAMN02745975_01194 {ECO:0000313|EMBL:SHJ05612.1};
OS Geosporobacter subterraneus DSM 17957.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Geosporobacter.
OX NCBI_TaxID=1121919 {ECO:0000313|EMBL:SHJ05612.1, ECO:0000313|Proteomes:UP000184536};
RN [1] {ECO:0000313|EMBL:SHJ05612.1, ECO:0000313|Proteomes:UP000184536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17957 {ECO:0000313|EMBL:SHJ05612.1,
RC ECO:0000313|Proteomes:UP000184536};
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; FQZV01000013; SHJ05612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6G6P6; -.
DR STRING; 1121919.SAMN02745975_01194; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000184536; 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; 1.10.8.60; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR046843; LonB_AAA-LID.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046:SF46; ARCHAEAL LON PROTEASE; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF20436; LonB_AAA-LID; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
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 ECO:0000313|EMBL:SHJ05612.1};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 138..333
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 370 AA; 41746 MW; CA90438B939B61E6 CRC64;
MWRLLYTLDE EFEKLFKIKV DFDDRMDTGE ENELSIAQFI SYYCKKKNIR HLDTTGVAKV
VEYCSRIAGS QKKLSTQFSK IAELLIEADV WAEVEREPYI CDRHIKKAYD EKIYRNNMLE
DRMLEMYKTK KIIIDIRDRK IGRINGLSVI NLGDHVFGKP SVITATTFIG HKGVINIERE
VEMSGSIHDK GVMILEGYLN ERFAQEAPLS LTGKICFEQS YGGVDGDSAS STELYALLSS
LGDVPLKQYI AVTGSVNQKG EVQPVGGVTE KIEGFFDICS YFGLTGDQGV MIPYQNVEDL
VLKDDVIDAV QKGLFHIYPV SSIEEGIEIL TDRSYPDIYE GIRAKLNKYA ASENQNTSST
KNGRESGNLL
//
