ID A0A0Q3TBT1_9BACI Unreviewed; 344 AA.
AC A0A0Q3TBT1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=AN964_19625 {ECO:0000313|EMBL:KQL51574.1};
OS Heyndrickxia shackletonii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL51574.1, ECO:0000313|Proteomes:UP000051888};
RN [1] {ECO:0000313|EMBL:KQL51574.1, ECO:0000313|Proteomes:UP000051888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL51574.1,
RC ECO:0000313|Proteomes:UP000051888};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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}.
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:KQL51574.1}.
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DR EMBL; LJJC01000006; KQL51574.1; -; Genomic_DNA.
DR RefSeq; WP_055741877.1; NZ_LJJC01000006.1.
DR AlphaFoldDB; A0A0Q3TBT1; -.
DR STRING; 157838.AN964_19625; -.
DR PATRIC; fig|157838.3.peg.4333; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000051888; 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 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 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; 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:UP000051888};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 119..164
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 230..340
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 283
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 344 AA; 37663 MW; C6989D6588176297 CRC64;
MNKSLKRKST LAFFIIIIVL IIGLFIPTPY YLEQPGSVEK LSPRVTVQDG HKDEKGNLYL
TTVLSTKATN VYIYLYGLMA PHTQMEKAQD VKGDMSDAEY DRLLEHMMSS SQQNAITSGL
KAAGQKVNVQ NNGVFVYAVL PDSKAKGTIK VGDIIHSVDG HPVKKSVDFI HYLSNKKAGD
TVQLGWTHDG KNETTTIPLV TLDKKTKRAG IGIVPEDEFT IQPSKKININ ASDIGGPSAG
LMFSLEIYNQ IVPGDLTKGY QIAGTGTIDQ NGNVGQIGGI RDKIVAAHKA GIDIFFCPAD
IQKGDTNEKD IKDEAHKLGY KIKIVPVKTM KDAIHYLEKL PPKK
//
