ID N1ZEW2_9CLOT Unreviewed; 804 AA.
AC N1ZEW2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-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 Name=lon {ECO:0000313|EMBL:USF29907.1};
GN ORFNames=C820_001327 {ECO:0000313|EMBL:USF29907.1}, C820_02773
GN {ECO:0000313|EMBL:EMZ11109.1}, FMM67_13285
GN {ECO:0000313|EMBL:NDO47775.1};
OS Clostridium sp. MD294.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=97138 {ECO:0000313|EMBL:EMZ11109.1};
RN [1] {ECO:0000313|EMBL:EMZ11109.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|EMBL:EMZ11109.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:NDO47775.1, ECO:0000313|Proteomes:UP000462571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|Proteomes:UP000462571}, and MD294
RC {ECO:0000313|EMBL:NDO47775.1};
RA Elie C., Mathieu A., Saliou A., Darnaud M., Leulier F., Tamellini A.;
RT "Draft genome sequences of 15 bacterial species constituting the stable
RT defined intestinal microbiota of the GM15 gnotobiotic mouse model.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF29907.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF356 {ECO:0000313|EMBL:USF29907.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) 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}.
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DR EMBL; AQFQ01000029; EMZ11109.1; -; Genomic_DNA.
DR EMBL; VIRC01000023; NDO47775.1; -; Genomic_DNA.
DR EMBL; CP097810; USF29907.1; -; Genomic_DNA.
DR RefSeq; WP_004038778.1; NZ_VIRC01000023.1.
DR AlphaFoldDB; N1ZEW2; -.
DR STRING; 97138.C820_02773; -.
DR PATRIC; fig|97138.3.peg.2785; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_0_1_9; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000012445; Chromosome.
DR Proteomes; UP000462571; 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; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000313|EMBL:USF29907.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000012445};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 571..766
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 188..215
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 535..562
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 661
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 704
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 804 AA; 90980 MW; E2319592801BF970 CRC64;
MPQTKELNYK QLKNICSPSD FSFQTTEEIS SLDGGVIGQE RAVKAFDFGL TVKMQGYNIF
MTGPSGTGKT TYAKISTKKI AATEPVPYDW CYVYHFQNPR TPLALRFKAG MGKQFKEDMS
ELVQIFKTEI QKVFRSEDYE KEKSVILKKF DEKKDIYMKE MSDMAKENGF QLRSSNSGIY
FMPIIDGKTI NEEEYDKLEE EQQEAIDKAS NVVQEKAGTI MRDLRELEKE CKKQTDDLDY
KVGMFAIGHH VNSVQEKYKE YTRVISYIND VKEDVLENIS QFFEEEEEVD ESIASLLPLF
SKKSSEDITQ KYKVNLIVDH SETEGAPVVV HFNPTYYNLV GEVEYDSEFG NLTTDFMKIK
AGLFHKANGG YLILQAQDIL SNPQSWEAIR RVIKTKEIAM DNLREQMGAI VAPVLKPEPV
PADFKIILIG SEYYYDVLSE FDDEFDKFFK IKAEFDYEMK RNDENIVKLA QFIKKFSEKE
HTAHFTADAV CAVIEYSSRT AERQDKLSTR FNRLTEVMGE AAAWAKLSGD TLITAKHIKK
AIEQKEQRLK MYEEKLGEML DEKVIMIDTE GSKIGQINGL AVLDMGSYAF GNPCRITATT
YMGESGIINI EKEAQLSGQT HDKGIQILTG FLGQTYAQEF PLSLSCRVCF EQNYNGIDGD
SASSTELYCI LSSLAEVPIR QDLAVTGSIN QRGEIQAIGG VTYKIEGFFD LCKKRGLTGT
QGVIIPETNI KDLVLKDEVI EAVKQGAFHI YAISTLEEGI ALLMDMEAGQ KNKNGKYPAN
SVHGKVMKKL KAYYKGASGE KIEK
//
