ID I9L0G3_LACPE Unreviewed; 349 AA.
AC I9L0G3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=KCA1_1808 {ECO:0000313|EMBL:EIW13651.1};
OS Lactiplantibacillus pentosus KCA1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1136177 {ECO:0000313|EMBL:EIW13651.1};
RN [1] {ECO:0000313|EMBL:EIW13651.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCA1 {ECO:0000313|EMBL:EIW13651.1};
RX PubMed=23527145;
RA Anukam K.C., Macklaim J.M., Gloor G.B., Reid G., Boekhorst J., Renckens B.,
RA van Hijum S.A., Siezen R.J.;
RT "Genome Sequence of Lactobacillus pentosus KCA1: Vaginal Isolate from a
RT Healthy Premenopausal Woman.";
RL PLoS ONE 8:E59239-E59239(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:EIW13651.1}.
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DR EMBL; AKAO01000045; EIW13651.1; -; Genomic_DNA.
DR RefSeq; WP_003639028.1; NZ_CM001538.1.
DR AlphaFoldDB; I9L0G3; -.
DR MEROPS; S16.012; -.
DR PATRIC; fig|1136177.4.peg.1430; -.
DR eggNOG; COG3480; Bacteria.
DR HOGENOM; CLU_042037_2_0_9; -.
DR Proteomes; UP000005826; 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; IPR036034; PDZ_sf.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000313|EMBL:EIW13651.1};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 231..347
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 349 AA; 38616 MW; 526ACD338D5EFBE4 CRC64;
MKTVQRLWKR YWGLVLIVVA LLIFFLLPLP YYIEGPGSAD NLKSFVTVKH HPDKRRGKFM
LTSVAEAPAT PALWLYAQLN PHYDVVSAED MTGGQDDATY NRVQKFYMRS AINEAIATAY
SAALQSYRTT YQGIYVLDIQ SNSKFKHQLK VGDTITKVDG HHFNTASAYQ RYISKQGVGH
RVTISYRRNG KTKQATAPLV KLSTHRAGIG ITLTDNVKVT TKIPVKVDPG QIGGPSAGLM
FSLQIYQQLT NQNLRHGQKI AGTGTIDQNG QVGEIGGIDK KVIAAKRAGA TIFFAPYVKP
TKALLAVEEQ GKTNYQLAKA TAKKYAPNMK VVPVTSFKQA VHYLQTHSK
//