ID A0A2C9T1V8_9MYCO Unreviewed; 332 AA.
AC A0A2C9T1V8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=MSZK_47090 {ECO:0000313|EMBL:GAY17983.1};
OS Mycobacterium sp. shizuoka-1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=2039281 {ECO:0000313|EMBL:GAY17983.1, ECO:0000313|Proteomes:UP000223528};
RN [1] {ECO:0000313|EMBL:GAY17983.1, ECO:0000313|Proteomes:UP000223528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=shizuoka-1 {ECO:0000313|Proteomes:UP000223528};
RA Yoshida M., Izumiyama S., Fukano H., Sugiyama K., Suzuki M., Shibayama K.,
RA Hoshino Y.;
RT "Draft genome sequence of Mycobacterium sp. shizuoka-1.";
RL Submitted (OCT-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY17983.1}.
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DR EMBL; BEWG01000093; GAY17983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9T1V8; -.
DR Proteomes; UP000223528; 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 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.
DR PROSITE; PS50106; PDZ; 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:UP000223528};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 104..182
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 225..323
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 332 AA; 34767 MW; 6B924EE6D67A2382 CRC64;
MTALVPIVVF GVLLAVVTVP YVSLGPGPTF DTLGEVDGKQ VVAIEGTPTQ PTSGHLNMTT
VAQRDGLTLG QALTLWVSGR EQLVPRDLVF PPEKSREDVE KDQDADFKRS EDSAEYAALG
YLKYPEAVRV EKVNDPGPSA GKLQAGDAID AVDGTKVANV AEFTGLLKAT KPGQEIVIDY
RRKNAPAGTA RITLGTNPDR DYGYLGVAVL DAPWAPFSID FNLANIGGPS AGLMFSLAVI
DKLTTGDLNG SKFVAGTGTI NEDGKVGPIG GITHKMLAAQ EAGATVFLVP ADNCDEAKSM
RDDSMELVKV DTLAGAVDSL HTLTSGGRPP SC
//
