ID A0A1G8U9E0_9GAMM Unreviewed; 797 AA.
AC A0A1G8U9E0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Lon protease {ECO:0000256|PIRNR:PIRNR001174};
DE EC=3.4.21.53 {ECO:0000256|PIRNR:PIRNR001174};
GN ORFNames=SAMN04488540_10917 {ECO:0000313|EMBL:SDJ50426.1};
OS Ferrimonas sediminum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=718193 {ECO:0000313|EMBL:SDJ50426.1, ECO:0000313|Proteomes:UP000199527};
RN [1] {ECO:0000313|EMBL:SDJ50426.1, ECO:0000313|Proteomes:UP000199527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23317 {ECO:0000313|EMBL:SDJ50426.1,
RC ECO:0000313|Proteomes:UP000199527};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|PIRNR:PIRNR001174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR001174}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family.
CC {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
CC ECO:0000256|RuleBase:RU000591}.
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DR EMBL; FNEM01000009; SDJ50426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8U9E0; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000199527; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 2.30.130.40; LON domain-like; 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; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001174};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR001174};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001174,
KW ECO:0000256|PIRSR:PIRSR001174-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001174};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001174}.
FT DOMAIN 30..227
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 616..797
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 704
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 747
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 382..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 797 AA; 88527 MW; FB3D558273832F12 CRC64;
MHQEDIDVID NDEPQPTDIV VAGEQRPDQL HVMPVQNRPF FPAQVMPVLI KSGDWIETLK
AVGETDHKML ALFYSEDFDH QEGRFNPQTL PQTGCVVRVH QVKEGDDGDI QFIAEGIERV
HIDSWESTSH PYLANVSYPE TEQDSEGKEI KAYAMALINA IKELLPINPL LSEELKDYLN
RFGPNEPSPL TDFGAAITTA PGPLLQEVVD QVALLPRMEK TLALLKKELD AARLHSEIAE
EVNRKISKHE REFFLREQLR VIQKELGVAK DDKTADLEEF NARMQGKTLP EAAEKKFKEE
MQKFSVLESG SPEYAVSRNY LDWITQMPWG IHSTDKLELS QARTILDKHH DGLDDVKDRI
LEFLALGAFK GEISGSIILL VGPPGVGKTS IGRSIAECLD RPFYRFSVGG MRDEAEIKGH
RRTYIGAMPG KLVQALKEAE VMNPVIMLDE IDKMGSSYQG DPASALLETL DPEQNVNFLD
HYLDLRLDLS KVLFVCTANT LDSIPAPLLD RMDVIHLSGY LAEEKLAIGK HHLWPRQLKR
AGVKRSQLKI TDAALKKVVV DYCREAGVRS LDKALAKLVR KSVVKLLQDP QQKLSLGLKA
IPELLGPAKF KAEQTLCGTG IVTGLAWTSV GGATLPVEAN SIHQQSRGLK LTGQLGDVMK
ESAEIAFSFI SSHLSQYDVE ENYFDKRFVH LHVPEGATPK DGPSAGITMS TALLSLALGK
APKKHLAMTG EITLNGYVLA VGGIREKLIA AKRQGIKEVL LPEECSGDYQ ELPDHVKEGL
KVHFVSHFDQ VAKLAFD
//
