ID A0A1I2JHJ9_9CLOT Unreviewed; 766 AA.
AC A0A1I2JHJ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=SAMN04487885_10247 {ECO:0000313|EMBL:SFF53749.1};
OS Clostridium cadaveris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1529 {ECO:0000313|EMBL:SFF53749.1, ECO:0000313|Proteomes:UP000182135};
RN [1] {ECO:0000313|EMBL:SFF53749.1, ECO:0000313|Proteomes:UP000182135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLAE-zl-G419 {ECO:0000313|EMBL:SFF53749.1,
RC ECO:0000313|Proteomes:UP000182135};
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}.
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DR EMBL; FOOE01000002; SFF53749.1; -; Genomic_DNA.
DR RefSeq; WP_074844208.1; NZ_JAUDCX010000004.1.
DR AlphaFoldDB; A0A1I2JHJ9; -.
DR STRING; 1529.SAMN04487885_10247; -.
DR eggNOG; COG1067; Bacteria.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000182135; 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; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR027417; P-loop_NTPase.
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:SF46; ENDOPEPTIDASE LA; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 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|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000182135};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 549..744
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 639
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 682
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 766 AA; 87334 MW; D76CF50B5143D954 CRC64;
MKRKLTSKEV IFQFDFKGED MDLSKDCVLH EYKDVYKEIE EIVLHDEKGD LNIYLVDEFS
KDKINDLISR IEEILKGKNP PKDICYVIYD NEKAPKVLIL KNGMAVKLKE SLEFVKEEVY
KIILKFYSTS SANDKDLIMD ELNKKRSDLI EFLMEKAKDE GFDIKATSQG FAFMPLKEEG
EAMTTKEYDG LDMLLKEEIL GKVSKLKSSA QDILDSIREL EDKYLDKVKM IMKTYLDDKS
KDIKDQYYKD LNGDEVSMNY LEFVINNIID SAVDNFSGEL DDDAEVIDKI IEKFIVNIIA
DNSGEKHPRV IFESNPTVSN LMGKIEYETQ SGTYATSPSL IYGGSLIRAN EGVFIVRISD
LLNNAGSYEY LNKAIFNKKI SYDFYRSYLE ILSLSTLDIE EIPFDTKIII IGDFEYYNIL
SEYDSNFKSN FPIHLEANPV IRICKEDMED IRVRLNKIIK DNNLLQITHG GFKEIVKYLC
RKSENRDKIY FNDEDVVRLL QRCCIKAKIS GKNQIDEASI QKITEEKSIF EIENIDMYKE
GKVLINVDGT KTGSVNGLSV VGTNNISFGK PIRITCVCYK GDGNILDAHK ESKLSGKIHE
KSLNILKAYI NSLYGKYNSL PVDFYLSFEQ VYGNLEGDSA SVAEVIAMLS ALTSISINQN
IAVTGSINQF GEIQPVGGIN EKIEGFFNLC DSISTIDGKG VLIPATNLSD IILNHKVEEA
VRKGEFSIYT MNTIEDAVEI LMEDMNWSRF MEISNNEIKR FIGKKK
//