ID A0A380MXN5_9GAMM Unreviewed; 625 AA.
AC A0A380MXN5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN Name=lon_1 {ECO:0000313|EMBL:SUO97042.1};
GN ORFNames=NCTC10717_01343 {ECO:0000313|EMBL:SUO97042.1};
OS Suttonella indologenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Suttonella.
OX NCBI_TaxID=13276 {ECO:0000313|EMBL:SUO97042.1, ECO:0000313|Proteomes:UP000254575};
RN [1] {ECO:0000313|EMBL:SUO97042.1, ECO:0000313|Proteomes:UP000254575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10717 {ECO:0000313|EMBL:SUO97042.1,
RC ECO:0000313|Proteomes:UP000254575};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; UHIA01000004; SUO97042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380MXN5; -.
DR Proteomes; UP000254575; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 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; IPR004815; Lon_bac/euk-typ.
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 NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF56; 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; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000313|EMBL:SUO97042.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000254575};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 420..600
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 18..82
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 506
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 549
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 625 AA; 69977 MW; BC457C6EE5FD4A4D CRC64;
MDIPVEARIN ILGTLNIQQR LEQVLILLEE EKDKAKLEQR IKKRVKEQMD KNQREYYLNE
KIKAIQKELN DLDENQLSET EQLEAQIKEA KMPAAAEKKA VGELNKLKQM SPMSAEATVI
RNYLEWMIDY PWSKRKRSQY DLEKAEAIFD RDHYGLADVK ERIIEYLAVQ KRNKNNKSPI
ICLVGPPGVG KTSLGKSVAE ATGRDFDRIS LGGVHDEAEI RGHRRTYIGA LPGKIVQKMC
KLGSNNPVIL LDEIDKIGSD HRGDPASALL EVLDPAQNSS FSDHYLETDI DLSKVLFIAT
ANTLNIPAPL LDRMEVIRIP GYTTREKLHI AERYIVPRQR KENALSEKEF VLQKGVLNQV
VEDYTREAGV RNLEREIGKL ARKAVRKLHD KSVKSVKITR DNLEDYLGVA KYRRSDEDLA
PKIGSVTGLA WTSVGGELLQ IETAAFSGKG KLTHTGQLGD VMKESIQAAL TVVRHYLEAH
DSDFRFADYD LHMHLPEGAT PKDGPSAGIA MATALLSAFT RSKVRGDIAM TGEITLHGRV
LAIGGLKEKL LAAQRGEIRT VLIPSDNVKD LRDVPEDVKK DLEIIAVSHV SEVFARVFAE
ESTPSKAFIP VQSLQNDGNM SKHAH
//
