ID A0A126T6G0_9GAMM Unreviewed; 798 AA.
AC A0A126T6G0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=JT25_014435 {ECO:0000313|EMBL:AMK77661.1};
OS Methylomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK77661.1, ECO:0000313|Proteomes:UP000030512};
RN [1] {ECO:0000313|EMBL:AMK77661.1, ECO:0000313|Proteomes:UP000030512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK77661.1,
RC ECO:0000313|Proteomes:UP000030512};
RX PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA Kits K.D., Klotz M.G., Stein L.Y.;
RT "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT FJG1.";
RL Environ. Microbiol. 17:3219-3232(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}.
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DR EMBL; CP014476; AMK77661.1; -; Genomic_DNA.
DR RefSeq; WP_062328965.1; NZ_CP014476.1.
DR AlphaFoldDB; A0A126T6G0; -.
DR KEGG; mdn:JT25_014435; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000030512; 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; 1.
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:SF46; ARCHAEAL LON PROTEASE; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 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:UP000030512};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 562..757
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 652
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 695
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 798 AA; 89178 MW; 5F1CB2BE04D02E37 CRC64;
MKIKPLSPAQ LYTPCKLEQL PFKTTDELDD VDSVLGQERA IAAIKFGIRL DKPGYNIFAM
APDGTGKLTT IKQLAEHEAC RQPVPSDWCY VHNFKQPAKP KAIWLEPGEG KGFQEDMAEL
IDELSVGIPA AFDGDEYRSR AGELENESRQ REIEVLNKLR EEAEQAHIIF TETANGYAFL
PANDDNEPYA PEQFNKLDKE RQHQFHDTVL ALQEKVQDAI KKFPQWRKQT KRKLQALNRE
VAELAVHHSI DDLKDKYAKH QAVLDYLSAV QQDIIDHVRD FIPHSDKVLS FMELPQDPNP
FKRYQVNLMV DLNHKRAAPV ICEDLPNHGN LLGRIDHQAQ MGSLVTDFTM IKPGAFHKAN
GGYLILDARK LLLQPYAWET LKRTLQAGEI RIESLERALS LISTSSLEPE PIPLNIKVIL
LGDPLLYYLL SFYDPEFQDF FKVAADFAGH VDREHNSLEY ARLLATIARR EKLRPLSQQA
VARIIEHSAR MADDSEKLLT HLRSIKDLLT EADYWAGENG HTVIANSDVQ QAIDEKNHRL
DRIRERLYET IQRGTIMIAT EDKVVGQING LSVLQLGEFS FGQPSRITAT TRMGNGKVVD
IERETELGGA IHSKGVLILS SFIASRYART RPFSLAASLV FEQSYGHVEG DSASLAELCA
ILSSLAQVPL RQDLAMTGSV NQLGQVQPIG GVNEKIEGFF DICAARGLSG SQGVIIPASN
IPHLMLRWDV VHAAQAGQFH IYQVATVDDA LGLLSDMDVG MADAQGQFPG DSFNGKIDAQ
LQQFTSLVKE FAAKADGK
//
