ID D3Q3V8_STANL Unreviewed; 355 AA.
AC D3Q3V8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=Snas_4378 {ECO:0000313|EMBL:ADD44025.1};
OS Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS NBRC 102104 / LLR-40K-21).
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Stackebrandtia.
OX NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD44025.1, ECO:0000313|Proteomes:UP000000844};
RN [1] {ECO:0000313|EMBL:ADD44025.1, ECO:0000313|Proteomes:UP000000844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX PubMed=21304662; DOI=10.4056/sigs.47643;
RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT 40K-21).";
RL Stand. Genomic Sci. 1:292-299(2009).
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; CP001778; ADD44025.1; -; Genomic_DNA.
DR AlphaFoldDB; D3Q3V8; -.
DR STRING; 446470.Snas_4378; -.
DR MEROPS; S16.012; -.
DR KEGG; sna:Snas_4378; -.
DR eggNOG; COG3480; Bacteria.
DR HOGENOM; CLU_042037_1_0_11; -.
DR Proteomes; UP000000844; Chromosome.
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; 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.
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:UP000000844};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 246..344
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 355 AA; 37803 MW; B5AEFBE467A58830 CRC64;
MRRRGLTVLI GAILVSVMTW QALSMRVAYV GLGPGPTYDA LAEYTFKDDD GKKKTVELIS
ADEKYSSKSK GQLRLVTVRI HDDIELARAL YYWLSDDYAV VPRELQFPED KSDEEIAAEQ
EEMWENSQAA AETAALRELG EEVEVTVTKV DSDSPSKGDL KRDDVITAVD GEEVTSQERL
AELLAAAAAK APGEAVKLTV DRDGKDKKVK VTPEENSQGV AILPGVDVEP KQKDPYGLKV
TAEGLNVGGP SAGLIFALAM VDRVSKEDLT GGADIIGTGE IDEDGNVGAI GGIAQKVVAA
SQQGAKVFLT PADNCAAAKA NVPDGLKLIK VSTLDGALKE LETLREGGEP TTCLT
//
