ID A0A1Y4GG54_9BACT Unreviewed; 844 AA.
AC A0A1Y4GG54;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=B5F39_03075 {ECO:0000313|EMBL:OUO94863.1};
OS Cloacibacillus sp. An23.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Cloacibacillus.
OX NCBI_TaxID=1965591 {ECO:0000313|EMBL:OUO94863.1, ECO:0000313|Proteomes:UP000196418};
RN [1] {ECO:0000313|Proteomes:UP000196418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An23 {ECO:0000313|Proteomes:UP000196418};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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}.
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:OUO94863.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NFJQ01000002; OUO94863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4GG54; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000196418; 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 Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000196418};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 581..776
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 815..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..265
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 671
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 714
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 844 AA; 94552 MW; F66D8A3942C166C8 CRC64;
MSLSEDRKLP ASSLRRQANL SALGFRTTKG LDKLSGLIGQ ERAVRSVNFG LSVQSKGYNI
FMVGEPGCGR TTYALEELRH AAASMPAPDD WVYVYNFDDP SVPLALRLPA GRGRELAKDA
ADAVEELKTA LSKAFDNNEF EDSKAHLVKA FQDEVNSIME ELRKWAESKN FAIKRTPQGF
VNLPLITAPP LPAPGSEAAE GEEPKEAEPV LREMQQEEFE KLSESEQAEL QKASEEISQK
TLEKLRLIRE KEKDLKEKIH ELESQICRVA IAPVMSELRT KYQPNEKLER WLDDFSEDLI
ANFNVFLAAV RDDQADVDFS RYEVNAFVSN NPNDGAPVVC ETNPIYYNLV GKVDYENRQG
NLYTDFRRIT PGAMHRANGG FLLLDADELL RQFMSWDVLK RVLRYRELAI ENLAEQLGYI
PVSSLRPEPI PVDMKVVIVG TPYLYYLLNI YDPEFSKVFK VKAEFDSEMP RTDESEMQIA
RFVAGFVERE GKLHFTAAAV GEVIEWASRL VEDKNKLSTQ LNKIAEVLVE STALAKGAGK
RQVGVEHVRN ALSEKLFRSD MWEEKVLDEY KNGVIRIDTD GFAVGQINGL TVSQLIDHSF
GSPVRITANV FMGTEGVVNI EREVRMTGPI HNKGLMTLTS YLGRMYAKKY PLSISARIAF
EQTYGGIEGD SASSTELYCL LSAIAEIPLN QGIAVTGSVD QRGNIQPIGG VNEKIEGFFR
YCEHNGLTGR QGVMIPVQNE RHLMLCHEVT EAVRKGKFHI WSISTIDEGI EILTGVPAGT
PDENGDYPKD SVHGRVQAAL EEWLERSFRY KKVIGDRIDP PKKKRQPKKE KASPESAGGG
REAE
//