GenomeNet

Database: UniProt
Entry: A0A2A2IVD4_9PSED
LinkDB: A0A2A2IVD4_9PSED
Original site: A0A2A2IVD4_9PSED 
ID   A0A2A2IVD4_9PSED        Unreviewed;       805 AA.
AC   A0A2A2IVD4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=CK486_10830 {ECO:0000313|EMBL:PAV48190.1};
OS   Pseudomonas sp. HAR-UPW-AIA-41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1985301 {ECO:0000313|EMBL:PAV48190.1, ECO:0000313|Proteomes:UP000243299};
RN   [1] {ECO:0000313|Proteomes:UP000243299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAR-UPW-AIA-41 {ECO:0000313|Proteomes:UP000243299};
RA   Kumari P., Krishnamurthi S.;
RL   Submitted (SEP-2017) 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:PAV48190.1}.
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; NSLB01000004; PAV48190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2IVD4; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000243299; Unassembled WGS sequence.
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; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR041699; AAA_32.
DR   InterPro; IPR046844; Lon-like_helical.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR046843; LonB_AAA-LID.
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   Pfam; PF20436; LonB_AAA-LID; 1.
DR   Pfam; PF20437; LonC_helical; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000243299};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          563..758
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          206..233
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        653
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        696
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   805 AA;  88413 MW;  467B9C89FDF3AFA9 CRC64;
     MAATAVAALK LQPEELTRPY SPDQFNFAST DELEPFRGVL GQERAVEALQ FGVAMPRPGY
     NVYVMGEPGT GRFSFVKRYL QAEAKRLATP ADWVYVNHFD DPREPRALQL PPGEGAQLIA
     DINQLIDNLL STFPAAFEHP TFQQKKNAID RAFNQRYDKA LDIIEKASLE KDVALYRDSA
     NVAFTPMKDG KALDEAEFAQ LPEAERERFH RDISALEEQL NEELASLPQW KRESSNQLRQ
     LNEETITQAL LPLLAPLSAK YAENASVVAY LQAMQVNLLK TVVDQMVEDN RSDAQRRRAL
     EEDYSPSLVV GHHAQGGAPV VFESHPTYDN LFGRIEYNTD QGALYTSYRQ LRPGALHRAN
     GGYLIVEADK LLSEPFVWDA LKRALHSRQL KMESPLGDLG RLATVTLTPQ VLPLQLKVVI
     VGSRELYYTL QDLDPDFQEM FRVLVDFDEE IALSDESLEQ FAQLLKTRTS EEGMAPLTGA
     AVARLATYSA RLAEHQGRLS ARIGDLFQLV SEADFIRHLA GDALTDVGHI ERALKAKADR
     TGRVSARILD DMLAGIILID TRGAAVGKCN GLTVLEVGDS AFGVPARISA TVYPGGSGIV
     DIEREVNLGQ PIHSKGVMIL TGYLGSRYAQ EFPLEISASI ALEQSYGYVD GDSASLGEVC
     TLISALSRTP LKQCFAITGS INQFGEVQAV GGVNEKIEGF FRLCEARGLT GEQGVIIPRA
     NVTNLMLDER VLQAVRGGQF HVYAVSQVDE ALSLLVGTDA GTPDEQGVFP EGSVNAQVVA
     RLREIAELGM EDDDKGKDKD KSDAS
//
DBGET integrated database retrieval system