ID B4EVD4_PROMH Unreviewed; 580 AA.
AC B4EVD4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=PMI0783 {ECO:0000313|EMBL:CAR41789.1};
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR41789.1, ECO:0000313|Proteomes:UP000008319};
RN [1] {ECO:0000313|EMBL:CAR41789.1, ECO:0000313|Proteomes:UP000008319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR41789.1,
RC ECO:0000313|Proteomes:UP000008319};
RX PubMed=18375554; DOI=10.1128/JB.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR41789.1; -; Genomic_DNA.
DR RefSeq; WP_012367739.1; NC_010554.1.
DR AlphaFoldDB; B4EVD4; -.
DR MEROPS; S16.A10; -.
DR EnsemblBacteria; CAR41789; CAR41789; PMI0783.
DR GeneID; 6800513; -.
DR KEGG; pmr:PMI0783; -.
DR PATRIC; fig|529507.6.peg.763; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_2_0_6; -.
DR Proteomes; UP000008319; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR027417; P-loop_NTPase.
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:SF49; LON PROTEASE HOMOLOG-RELATED; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
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|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 340..537
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 475
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 580 AA; 66149 MW; 54CE46BA7E19528D CRC64;
MKNNELEWQA LRPDYASYQT FFQTASQLPA SSLREVQPRL YESLQWLNNA EAGQFMLLKA
EDSTAYFETL ADTLQQAEIK TYPVVGAYQA ESNQIYWQDN VEGSFSSSES IACCQWIEPE
QLFGSFYYHK DKLLVNPGLL HKVNGGILVL SIKTLLAQPL MWFRLKKMVE EQRFEWLVWN
DHQALPLPIE AMPLHLRVIL VGDRLSLEEL EFMEPNISST ALYGEYEYDM YLEDETALSQ
WCGFVNGLCQ KYRLPSLSAD AWQVLLTQGA REHEDQLILS LDLEFILRQL RYAMRFNHDA
YLGAEALKKA QENRLWRHSY LLERSRDEIL QGQVTIHTEG EMVGQINGLS VLDYPGYPDL
IGEPTRITCV AHIGDGELVD IERKAELGGN IHAKGMMIMQ AYLNSELRLD QPQPFSASVV
FEQSYGEVDG DSASLAELCA LISTLSQHPI DQQIAVTGAV DQFGQVQPIG GVNQKIEGFF
DICQQRGLTG SQGVIIPLAN VRHLVLNDSV IQAVKENKFH IWPVVHVAEA ITLLTHQPYY
EEQCENPQSN EHLLAIIHDR ITQANNQDRP KLPWFLRLFR
//
