ID A0A0N0VIY5_9PSED Unreviewed; 812 AA.
AC A0A0N0VIY5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=PF66_04380 {ECO:0000313|EMBL:KPA89225.1};
OS Pseudomonas fuscovaginae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA89225.1, ECO:0000313|Proteomes:UP000037931};
RN [1] {ECO:0000313|EMBL:KPA89225.1, ECO:0000313|Proteomes:UP000037931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA89225.1,
RC ECO:0000313|Proteomes:UP000037931};
RX PubMed=26422147;
RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA Cruz C.V., Oliva R.;
RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL PLoS ONE 10:E0139256-E0139256(2015).
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:KPA89225.1}.
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DR EMBL; JSYZ01000017; KPA89225.1; -; Genomic_DNA.
DR RefSeq; WP_054059048.1; NZ_JTBY01000133.1.
DR AlphaFoldDB; A0A0N0VIY5; -.
DR STRING; 50340.PF66_04380; -.
DR PATRIC; fig|50340.43.peg.1685; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000037931; 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}; 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 812 AA; 88931 MW; 21B2941589DC740C CRC64;
MSDSVAASLR LAPEALTRPF SAEQFSFSTT NDLEPFRGVL GQERAVEALQ FGVAMPRPGY
NVFVMGEPGT GRFSFVKRYL KAEGKRLQTP SDWVYVNNFD EPREPRALEL PAGEAGAFIS
DIGGLIDNLL ATFPAVFEHP SYQQKKSGID RSFNQRYDRA LDVIERLALE KDVALYRDSS
NIAFTPMSDG KALDEAEFAQ LPEAERERFH TDIAELEERL NEELASLPQW KRESSNQLRQ
LNEETITLAL QPLLAPLSEK YAENAAVCGY LQAMQVNLLR TVVEQLVDDS KTDAVARKLL
EEQYAPSLVV GHPASGGAPV VFEPHPTYDN LFGRIEYSTD QGALYTTYRQ LRPGALHRAN
GGFLILEAEK MLSEPFVWDA LKRALQSRKL KMESPLGELG RLATVTLTPQ MIPLQLKVII
IGARHLYYTL QDLDPDFQEM FRVLVDFDED IPMVDESLEQ FAQLLKTRTS EEGMAPLTAD
AVARLATYSA RLAEHQGRLS ARIGDLFQLV SEADFIRHLA GDERTDAGHI ERALKAKATR
TGRVSARILD DMLAGIILID TDGAAVGKCN GLTVLEVGDS AFGVPARISA TVYPGGSGIV
DIEREVNLGQ PIHSKGVMIL TGYLGSRYAQ EFPLAISASI ALEQSYGYVD GDSASLGEAC
TLISALSKTP LKQCFAITGS INQFGEVQAV GGVNEKIEGF FRLCEARGLT GEQGAIIPQA
NVATLMLDEK VLQAVRAGMF HVYAVRQADE ALSLLVGEPA GEPDADGQFP EGSVNARVVE
RLRVIAELIS EDDLKEAEKE AAEQALAEVK PS
//
