ID I2NF06_9PAST Unreviewed; 545 AA.
AC I2NF06;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=HMPREF1054_0553 {ECO:0000313|EMBL:EIG24417.1};
OS Haemophilus paraphrohaemolyticus HK411.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095743 {ECO:0000313|EMBL:EIG24417.1, ECO:0000313|Proteomes:UP000003345};
RN [1] {ECO:0000313|EMBL:EIG24417.1, ECO:0000313|Proteomes:UP000003345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK411 {ECO:0000313|EMBL:EIG24417.1,
RC ECO:0000313|Proteomes:UP000003345};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (APR-2012) 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:EIG24417.1}.
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DR EMBL; AJMU01000067; EIG24417.1; -; Genomic_DNA.
DR RefSeq; WP_005709432.1; NZ_AJMU01000067.1.
DR AlphaFoldDB; I2NF06; -.
DR PATRIC; fig|1095743.3.peg.1560; -.
DR eggNOG; COG1067; Bacteria.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000003345; 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; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
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 PRINTS; PR00830; ENDOLAPTASE.
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}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 301..498
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 545 AA; 61437 MW; 9CF4161E7C1F31CA CRC64;
MHLSSLSWQS LFLHHSFKLS DQSVNFFDFQ PKAQQALNLF KSQEMGSLLV MKSEVLPEFL
DELSVQLSQD NSQPVIVRTE FKASHLFGYT LFLEKENRIE TIKGAIQQAQ NGILVLRLNT
LLHDLKQWDK LKQALLFGFY EQNAVNHVPE ALPAIQSPFK LLLVGSREDI SMLAAYDGDL
YQFAQYTEID SFLNVDEESL NQWGDYVQAY AQKFVQRRFT LKALNQLLQH YMRESESQTM
ISISPTKLKN QLLGFAKFYP NSTAFDEVNT YLEALELQAS TLNQYALQDI LNNQVYIETE
DEEIGQINGL SVIEFEGVPY AFGEPLRISC NVQYGDGEIT DIERKVELGG NIHSKGILIA
QSCLANLLEL PTQLPFSASL AFEQSYGEVD GDSSSLAIFC VLVSRLAKVA LPQSIAVTGS
IDQFGNVLSV GGVNYKIEGF FNLCAARGLT GKQGVVIPTS CISHLSLKSE VIEAVKAGQF
QIWAVESVFE AVEILLKNAF YAEDHREKSD KPALFDLIHQ GIEQSPNHDV EHKLWHKIFP
WWKSH
//
