ID C1CGQ0_STRZJ Unreviewed; 345 AA.
AC C1CGQ0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=SPJ_1961 {ECO:0000313|EMBL:ACO18902.1};
OS Streptococcus pneumoniae (strain JJA).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488222 {ECO:0000313|EMBL:ACO18902.1, ECO:0000313|Proteomes:UP000002206};
RN [1] {ECO:0000313|Proteomes:UP000002206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJA {ECO:0000313|Proteomes:UP000002206};
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000919; ACO18902.1; -; Genomic_DNA.
DR RefSeq; WP_000727268.1; NC_012466.1.
DR AlphaFoldDB; C1CGQ0; -.
DR MEROPS; S16.012; -.
DR KEGG; sjj:SPJ_1961; -.
DR HOGENOM; CLU_042037_2_0_9; -.
DR Proteomes; UP000002206; Chromosome.
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 Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; NF041438; SepM_fam_S16; 1.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000313|EMBL:ACO18902.1};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 229..344
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 345 AA; 37552 MW; 5EB93A58589C0095 CRC64;
MKKKIRWPLY VIAALIVTFL AFVVPLPYYI EVPGGSEDIR QVLKINDTED KEAGAYQFVT
VGVQHATLAH MIYAWLTPFT DIRSAQETTG GSSDVEFMRI NQFYMQTSQN MAKYQGLKTA
GKDIELKYFG VYVLNVTDNS TFKGILNISD TVTAVNDQTF DSSKDLIDYV SSQKLGDSVK
VTYEEDGQTK SAEGKIITLE NGKNGIGIGL IDRTEVISNV PISFSTAGIG GPSAGLMFSL
AIYTQIAHPD LRNGRIVAGT GTIDRDGNVG DIGGIDKKVV ASARAGAAIF FAPDNPVSEE
EQKAHPDAKN NYQTALEAAK TIKTDMKIVP VKTLQDAIDY LKNNP
//
