ID Q9HVK8_PSEAE Unreviewed; 817 AA.
AC Q9HVK8;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=PA4576 {ECO:0000313|EMBL:AAG07964.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG07964.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG07964.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 ---------------------------------------------------------------------------
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; AE004091; AAG07964.1; -; Genomic_DNA.
DR PIR; F83073; F83073.
DR RefSeq; NP_253266.1; NC_002516.2.
DR RefSeq; WP_003112820.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; Q9HVK8; -.
DR SMR; Q9HVK8; -.
DR STRING; 208964.PA4576; -.
DR PaxDb; 208964-PA4576; -.
DR GeneID; 880974; -.
DR KEGG; pae:PA4576; -.
DR PATRIC; fig|208964.12.peg.4788; -.
DR PseudoCAP; PA4576; -.
DR HOGENOM; CLU_014785_0_1_6; -.
DR InParanoid; Q9HVK8; -.
DR OrthoDB; 9758568at2; -.
DR PhylomeDB; Q9HVK8; -.
DR BioCyc; PAER208964:G1FZ6-4669-MONOMER; -.
DR Proteomes; UP000002438; 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; 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 Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000002438};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 563..758
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 789..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 653
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 696
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 817 AA; 90223 MW; 511DFC722FF2CFCB CRC64;
MPDSVAAGLR LAPEELTRPF APEQFTFDTT DDLEPFRGVL GQERAVEALQ FGVAMPRPGY
NVFVMGEPGT GRFSFVKRYL QAEGKRVATP SDWVYLNNFD EPREPRVIEL PPGSATEFSA
DIDRLIDNLM STFPAVFEHP AYQQKKNAVD RAFNQRYDRA LDSVERRALE KDVALYRDSA
NVAFTPMKDG KALDEAEFAQ LPEAERERFH KDIAALEEYL NEELASLPQW KRESSNQLRE
LNEETITLAL QPLLAPLVEK YNNNPGVCAY LQAMQLNLLK TVVDQLVDDS RTDAQRKQGL
IEQYAPNQAI VHHATSGAPV VFESHPTYDN LFGRIEYSSD QGALYTSYRQ LRPGALHRAN
GGFLILEAEK MLGEPFVWDA LKRALQSRQL KMESPLAELG RLAAVSLTPQ VIPLQLKVII
IGSRQIYYTL QDLDPDFQEM FRVLVDFDED IPLGEDSLEQ FAQLLKTRTS EEGMAPLSGA
AVARLATYSA RLAEHQGRLS ARIGDLFQLV SEADFIRQLA NEEVIQLGHI ERALKAKQTR
TGRVSARILD DMLAGIILID TAGAAVGKCN GLTVLEVGDS VFGVPARISA TVYPGSSGIV
DIEREVNLGQ PIHSKGVMIL TGYLGSRYAQ EFPLEISASI ALEQSYGYVD GDSASLGEVC
TLISALSRTP LKQCFAITGS INQFGEVQAV GGVNEKIEGF FRLCEARGLT GEQGVIIPRA
NVTTLMLDER VLQAVRAGQF HVYAVREVDE ALALLVGKPV GAQDEKGRFP KGSVNDLVVA
RLQEISELGM EEDDKEKDKP AEKETVAAKD KAAAKKD
//
