ID A0A1T5J2R5_9MICO Unreviewed; 382 AA.
AC A0A1T5J2R5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=SAMN06309945_1145 {ECO:0000313|EMBL:SKC45572.1};
OS Okibacterium fritillariae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Okibacterium.
OX NCBI_TaxID=123320 {ECO:0000313|EMBL:SKC45572.1, ECO:0000313|Proteomes:UP000190857};
RN [1] {ECO:0000313|EMBL:SKC45572.1, ECO:0000313|Proteomes:UP000190857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2059 {ECO:0000313|EMBL:SKC45572.1,
RC ECO:0000313|Proteomes:UP000190857};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FUZP01000001; SKC45572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5J2R5; -.
DR STRING; 123320.SAMN06309945_1145; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000190857; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd00989; PDZ_metalloprotease; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Reference proteome {ECO:0000313|Proteomes:UP000190857};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..220
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 263..361
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 382 AA; 39966 MW; 9CFA7057F94B410E CRC64;
MTLFDDQPAS PVSPARSAQS RRRSAGWLSL AIAFVLLGVL ALWPSPWVIE QPGPVFNTLG
TVQHDKKDVP MIDIQGAETY DTAGSLDMLT VQVNGTPDQR PSWFEVAMSW FDPSRAVVPL
EAVYPPGVTT EQRSEQNATL MVDSQQDAVA AALSELGYTY PQHLAVGSVA TGSPAENVLK
VDDDLVSVNG ETVDDLESVR TAISANGADK AASIDIVRGG VPMTVEVTPI EQKDAAGDTQ
TVIGIGTRMV YDFPIDVTIQ LDNVGGPSAG MMFALGIIDK LTPGELNGGA DVAGTGTITE
SGEVGAIGGI RQKLFAARDD GATIFLAPSA NCDEVVGHVP DGIRVFSVST LKDSMAVLDA
VREKGDLDAL PTCETAAAAP TE
//
