ID G9WWZ6_9FIRM Unreviewed; 848 AA.
AC G9WWZ6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Lon protease {ECO:0000256|PIRNR:PIRNR001174};
DE EC=3.4.21.53 {ECO:0000256|PIRNR:PIRNR001174};
GN ORFNames=HMPREF9624_01370 {ECO:0000313|EMBL:EHL09329.1};
OS Oribacterium asaccharolyticum ACB7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=796944 {ECO:0000313|EMBL:EHL09329.1, ECO:0000313|Proteomes:UP000003527};
RN [1] {ECO:0000313|EMBL:EHL09329.1, ECO:0000313|Proteomes:UP000003527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACB7 {ECO:0000313|EMBL:EHL09329.1,
RC ECO:0000313|Proteomes:UP000003527};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Oribacterium sp. ACB7.";
RL Submitted (AUG-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHL09329.1}.
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DR EMBL; AFZD01000021; EHL09329.1; -; Genomic_DNA.
DR RefSeq; WP_009537150.1; NZ_JH414505.1.
DR AlphaFoldDB; G9WWZ6; -.
DR PATRIC; fig|796944.3.peg.2117; -.
DR HOGENOM; CLU_004109_4_4_9; -.
DR Proteomes; UP000003527; 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; 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; 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:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 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 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 ATP-binding {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-
KW 2}; Coiled coil {ECO:0000256|SAM:Coils};
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 661..839
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 32..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 186..213
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 32..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 745
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 788
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 425..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 848 AA; 94657 MW; 38DE0872C4859CF1 CRC64;
MKMNKLVEAL KKWIEKREEG VEKKGRISAI SREIPKTKGE ACSEKKSGEE DKNAEQAKSN
EKTGEALQAF SEEEKDRGGQ AMRVVPVYNM MILPNSYIYF QIDNFRTLAG KTVEEGDKLL
LAVLHKNEVD TRALHKEEVH PIGVEGTIKE ISKDGYAVVE TGNRVRIDAL SQVEGEPLLL
QTTPLYDVED VDREEAAKKL QEIKEELKGL VERFHAGKVM AGMIDHHQAI QEVACVLSPW
LSLNNEERYR VLQEDRLSVR TKMLEQIIYE YIEVTKVTTD ARTQQQEDYQ KLYKEQALQK
QIDYLQKELD EMHPEKVSDL RKFELRIAEA GMNETAKKEA GKILNRLKNE GTNGQEAGML
YDYLDFVTGL SWKKEEQKEI DLDEAEKILS EDHFGLKKVK ERMIQQIAVM NLKKQQSGSI
LLFVGAPGTG KTSIGKSIAK ALGRKYVRVS LGGVRDEADI RGHRRTYLGA MPGRIMDGIQ
KAGVSNPVMV LDEVDKLSAS YNGDPAAALL EVLDPEQNNT FTDHYMNVPY DLSDVLFICT
ANSLDTIPAP LLNRMEVIQY QGYTPKEKFE IAKRHLLRKS LKGVGLQQEN VEITDEALEN
IISDYTREAG VRGLKKRLDT LCRIAAVHLV KGKGEKISVG KGDLREYLDM NPLHRREVKE
EGKPGIVTGL AWTAVGGEIL YIESMFTKGE GKLNITGQLG DVMKESAQIA ISLVKSMFPD
KAKLFKENDL HIHVPDGATP KDGPSAGITL TIALASLVTG QAVSPRIAMT GEVSLEGLVN
PIGGLPEKLM AAERAGVKTV LIPKANEDDL RDVPDEVKEK LQILPVKTVE EGLELCEIKY
TKSGLEVV
//
