ID A0A348AHS3_9FIRM Unreviewed; 646 AA.
AC A0A348AHS3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN Name=lon2_2 {ECO:0000313|EMBL:BBB90621.1};
GN ORFNames=MAMMFC1_01275 {ECO:0000313|EMBL:BBB90621.1};
OS Methylomusa anaerophila.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Methylomusa.
OX NCBI_TaxID=1930071 {ECO:0000313|EMBL:BBB90621.1, ECO:0000313|Proteomes:UP000276437};
RN [1] {ECO:0000313|EMBL:BBB90621.1, ECO:0000313|Proteomes:UP000276437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMFC1 {ECO:0000313|EMBL:BBB90621.1,
RC ECO:0000313|Proteomes:UP000276437};
RX PubMed=29458677; DOI=10.1099/ijsem.0.002635;
RA Amano N., Yamamuro A., Miyahara M., Kouzuma A., Abe T., Watanabe K.;
RT "Methylomusa anaerophila gen. nov., sp. nov., an anaerobic methanol-
RT utilizing bacterium isolated from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 68:1118-1122(2018).
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; AP018449; BBB90621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348AHS3; -.
DR KEGG; mana:MAMMFC1_01275; -.
DR OrthoDB; 2318150at2; -.
DR Proteomes; UP000276437; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR014252; Spore_LonC.
DR NCBIfam; TIGR02903; spore_lon_C; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF64; LON PROTEASE; 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; PS50045; SIGMA54_INTERACT_4; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000313|EMBL:BBB90621.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000276437};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 196..377
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 467..640
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 550
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 593
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 646 AA; 70964 MW; 8A15AB584B3CDCD5 CRC64;
MKEFFNKFVG RRRSMDSASN SNKEDQLKRQ VAALYGLYTG VMGAERVVLK AGKLGALDLM
RSEFMPERVL ALQKLVFEDP TVEKLPTFQE IPDILNEIED ELADLCARRT VEDRIEKKIA
EKMEERHQEY IQEIRAQVLK EESDSNAENP QTLKKYAMLE KLESRKLTKS AMELLRPARL
DEIVGQERAI EALRAKLASP YPQHLILYGP PGVGKTTAAR LVLEEAKNLK TTPFPKDAPF
VEADGTTLRW DPRDVTNPLL GSVHDPIYQG ARRDLAETGV PEPKPGMVTD AHSGILFIDE
IGEMDPMLQN KLLKVLEDKR VRFDSAYYDP SDPSVPKYIR KLFEEGAPAD FVLIGATTRD
AQDIMSAVRS RCAEIYFEPL APKNIEEIVY NAAAKLGVII EAEVPRLISE YTIEGRKAVN
ILADAYSLAL LDKGHKTTDV TISAQNVYRV AQVSRLTPYV NLKASATAEV GKVFGLGVSG
YLGSVLEIEA IAFATEKGRG NIRFNDTAGT MAKDSVFNAA AVVRKITGED LANYDIHVNI
IGGGRIDGPS AGTAILAAII SAITGRPIRQ DVAVTGEVSI QGRVKAVGGV FEKAYGAKQA
GIRIMIIPAE NKVDIPEAHL GLDIRPIATV EEALAILLVD EQKSIA
//
