ID A0A0G0Z0W2_9BACT Unreviewed; 741 AA.
AC A0A0G0Z0W2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=UV05_C0044G0006 {ECO:0000313|EMBL:KKS42420.1};
OS candidate division CPR1 bacterium GW2011_GWA2_42_17.
OC Bacteria; candidate division CPR1.
OX NCBI_TaxID=1618341 {ECO:0000313|EMBL:KKS42420.1, ECO:0000313|Proteomes:UP000034875};
RN [1] {ECO:0000313|EMBL:KKS42420.1, ECO:0000313|Proteomes:UP000034875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:KKS42420.1}.
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DR EMBL; LCCZ01000044; KKS42420.1; -; Genomic_DNA.
DR PATRIC; fig|1618341.3.peg.618; -.
DR Proteomes; UP000034875; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
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:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
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.
DR PROSITE; PS01046; LON_SER; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 551..734
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 638
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 682
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 741 AA; 82772 MW; B824E49AAD10D045 CRC64;
MSRKPKRNRH GLPQKLMAFK SXXXXXXXXK IYIGLLNADR FKFLPSTTGL YVEIIKLNRD
KMQCSFIGRN RLEILSLDEL NFRKNSCAYA KIRLPKNRKI RSDEGVEVNH LRMDIDKCVA
SLLVGELWDW IKLIFTEQPG ALADKMAASG AISEPTDVQT IFYTLDPLSR LRIARNRLMV
LTEHLKRVAE EANYDTFQEG DVSQEDNELD FEKMFKKVKK FMLPELANVV EGRIREYRAS
LGQNDKVETY LRNVLGMPWG KIAKDPHRSI SQIRKQLDDD HYGLNKPKEK ILEFLAVRFL
NPDNKSSIIC LLGPPGVGKT SLGQSLGKKK ALNRPLVRIS VGGVHDEATI RGHGYTYQGS
AMGRIMQAVK QSGVMNPIIL IDEIDKVGEN GGNGNPAAAL LEVLDPLQNN RFVDHYFGGP
VDLSGVFFIL TGNNFMAINP ILRDRLHVAE IESYDMFEKL QIAKNFLVPK QLRSCGLDRV
LSFTDKALDV LIQGYTHESG VRELERKIEN ICANKARIIV ETQTRGRTKI DPKEVVSILG
PSEFIYDFSR ITPVGCCNGL AVVGHVGVLI VIETELISRR RAEVFTGVGD KIKDSVEKAL
SLLEGINPAF KEKIKKHFSE GGTHFNIGDG NINADGPSAG IAILCALFSL FSGKPVRERL
AMTGAINLTG GDVGVVGGIK EKVTGAMNAG INELILPAHN RSRFEKIDKR ITNKFKKVHF
VKSVDEVLTI VFGKDYKKIK V
//
