ID N0DYM0_9MICO Unreviewed; 343 AA.
AC N0DYM0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=BN10_190003 {ECO:0000313|EMBL:CCH69527.1};
OS Phycicoccus elongatus Lp2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1193181 {ECO:0000313|EMBL:CCH69527.1, ECO:0000313|Proteomes:UP000013167};
RN [1] {ECO:0000313|EMBL:CCH69527.1, ECO:0000313|Proteomes:UP000013167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lp2 {ECO:0000313|EMBL:CCH69527.1,
RC ECO:0000313|Proteomes:UP000013167};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH69527.1}.
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DR EMBL; CAIZ01000085; CCH69527.1; -; Genomic_DNA.
DR RefSeq; WP_010849454.1; NZ_HF570956.1.
DR AlphaFoldDB; N0DYM0; -.
DR STRING; 1193181.BN10_190003; -.
DR eggNOG; COG3480; Bacteria.
DR HOGENOM; CLU_042037_1_0_11; -.
DR Proteomes; UP000013167; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000013167};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 233..330
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 343 AA; 34765 MW; B44536B09C26EEE7 CRC64;
MVVSLVAAFL VLAVAAVLAI VPLPYAVMSP GPVTDTLGSL GDQKIIDVAG EGQHPEKGRL
FFTTVRVQGG PGTRVTAYDL LGAALDDSRD VYPQDEIFPP SSTRESVQQE NAAEMEGSQQ
TAAAVAERAL GHDVPVSVLV AQVLKGSPSD GLIEADDVLV SVDGIPASSP EAVRTAVRAH
KPGDEVSVTV RRAGSEVTVA PRAADTRGVA TIGVVMSGRY QLPIPVTIHA GAVGGPSAGL
MFSLGIYDVL TEGNLTGGAS IAGTGTIADD GAVGPIGGIR QKVVGAREAG ATWFLTPADN
CADLKGHVPA GLHLVKVATF SDAKQAVESI AAGSTDTLSS CGF
//
