ID A0A0D7CDW8_9ACTN Unreviewed; 365 AA.
AC A0A0D7CDW8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=SNA_34360 {ECO:0000313|EMBL:KIZ14196.1};
OS Streptomyces natalensis ATCC 27448.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1240678 {ECO:0000313|EMBL:KIZ14196.1, ECO:0000313|Proteomes:UP000032458};
RN [1] {ECO:0000313|EMBL:KIZ14196.1, ECO:0000313|Proteomes:UP000032458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27448 {ECO:0000313|EMBL:KIZ14196.1,
RC ECO:0000313|Proteomes:UP000032458};
RA Mendes M.V., Beites T., Pires S., Santos C.L., Moradas-Ferreira P.;
RT "Draft genome sequence of Streptomyces natalensis ATCC 27448, producer of
RT the antifungal pimaricin.";
RL Submitted (SEP-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}.
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:KIZ14196.1}.
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DR EMBL; JRKI01000061; KIZ14196.1; -; Genomic_DNA.
DR RefSeq; WP_030067771.1; NZ_JRKI01000061.1.
DR AlphaFoldDB; A0A0D7CDW8; -.
DR PATRIC; fig|1240678.4.peg.7319; -.
DR Proteomes; UP000032458; 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; 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 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 250..348
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 365 AA; 37806 MW; DE3A714804F089ED CRC64;
MPRRLATLLA STLMLIALLI AGVLIPVPYS EMSPGPTVNT LGDHAGAPVL QISGRKTYQP
TGHLNMTTVR VTGPDYRMNA FEAFIGWLGH DSTVVPHKTL YPEGQTAEQA DQENAEEFSQ
SQESAKVAAL GQLHIPVASQ TVVASVMKDK PADGKLHAGD VIKAVDGKPV RTYGDVAKLV
TRHKPGEKTV FTVIPAKVAA AAEKQGKRPA GDQKQVALTT TKADNGRAVV GIQAGVDHIF
PFPIDIKLAD VGGPSAGLMF ALGIVDKLTP GNMTGGRFVA GTGTIDDKGK VGPIGGISMK
TVGARAKGAQ FFLTPKENCA AAAKDTPEGL TLVKVGTIGD AVKALDKIST GHTAGLPSCS
PAGRS
//
