ID A0A1V1I3K9_9FIRM Unreviewed; 750 AA.
AC A0A1V1I3K9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=CRIB_2205 {ECO:0000313|EMBL:CED94806.1};
OS Romboutsia ilealis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=1115758 {ECO:0000313|EMBL:CED94806.1, ECO:0000313|Proteomes:UP000245622};
RN [1] {ECO:0000313|EMBL:CED94806.1, ECO:0000313|Proteomes:UP000245622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB {ECO:0000313|EMBL:CED94806.1,
RC ECO:0000313|Proteomes:UP000245622};
RA Hornung B.V.;
RL Submitted (APR-2014) 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; LN555523; CED94806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1I3K9; -.
DR Proteomes; UP000245622; Chromosome chr1.
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; 2.
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 Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000245622};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 530..725
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 96..147
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 750 AA; 85671 MW; FBC99822E5EA4A86 CRC64;
MLKFNNTSEI EPLEGILGQE RAIEAMEKGL KIDNPAYNMY LAGDSGTGKT TYAMSALNKY
AAKKGSHKDW CYVYNFENNR EPLIIGLEKG LGKIFKKDIE KLIETLLDEL RDAFESEDFE
IGKNQLIEEY EIEKDALLKK IKKYAEEKGF KLKNSKVGMV FMPIEENKED EEAEDDYADE
EFYKVKRELE NAAIQVVYKI RDLEDAAKEA LLELEEEIAK YVIDPHIDGL IEKYNGYEKV
KMYLNNMRDD ILEYVYLFYM DEEELKDKYD REHFMKYKVN LFVDNGIDRE NFKAPVIVEI
NPSPANLFGK AEYDYYNGNV KTDFTKLIPG AVHKANGGYL VLYVDQLLRY PLSWDMLKRA
IQSRQISVDT QTSIKPENMP IDIKVILIGT NYMYNLLYNN DDDFSKYFKI FVDFDNEMDK
NENNEDGIAR FIAYQCEKNK LKHFTYDAVG EVIKFSTRLC GDKYKLSTQF NKIMEIIVEG
DACAQIRNAE YVDKYDVQNA ILERKKRLNR IENKMDESLE NGFTLIETKG SRVGVINGLS
VLSTGEYSFG RPSRITVTTS PGNKGIVNIE REVNMSGPIH NKGVLILGGY LAETFAQDFP
LSLNANICFE QNYGGVDGDS ATGAELYALL SSLSKIPLKQ SIAATGSMNQ KGEIQVVGGI
SEKIEGFYST CKKQGLNGNQ GVIIPKNNSR NLVLSDEVTE AIETGKFTIY TVERVEEAME
ILMDVKFDEV KRLVIERLRG FNELQSPSKK
//
