ID R7RQ13_9CLOT Unreviewed; 786 AA.
AC R7RQ13;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=TCEL_00185 {ECO:0000313|EMBL:CDF58139.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58139.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF58139.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58139.1,
RC ECO:0000313|Proteomes:UP000014923};
RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT alkalithermophilic Caloramator celere.";
RL Submitted (MAR-2013) 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:CDF58139.1}.
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; CAVN010000095; CDF58139.1; -; Genomic_DNA.
DR RefSeq; WP_018661942.1; NZ_HF952018.1.
DR AlphaFoldDB; R7RQ13; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_0_1_9; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000014923; 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:0046982; F:protein heterodimerization activity; IEA:InterPro.
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; IPR009072; Histone-fold.
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; SSF47113; Histone-fold; 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 ECO:0000313|EMBL:CDF58139.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000014923};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 556..751
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 194..239
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 646
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 689
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 786 AA; 90634 MW; A680BBEE0A697B98 CRC64;
MSPIKKLSYE QLKTVFNLPK FKNTSEIKPE YQLIEQKRAI EAINFALEMD QFGYNIYVCG
YEGIGKRSYL IDMLKKRAKK EKTPSDWVYV YNFEDIYKPI ALELKPGTAY EFKQDINDFI
DNIIEELPEF ISSEEFEKKR NELIEYYEKI ILDLSNEINE KCKEKNLVFK YTNDGFAFIP
INKNNKEMTE QEYLELSDED RDEINKNVNE LKSAAYDVIR KTRNIKKELN QKIKDIENSL
CTLYIEGKMS NLIEKYSYSD KIKQYLNNLK LDIIENIDVF VEFENLDKEF VENFINRYEV
NVMVNNSIEG APVVIEETPE YQKLIGLVEY ENKSGNLVTD FTMIQPGSLH LANGGYLVLD
ARKLLESYFG YEALKRCLLL NKIIIENLKN QLDIIPIVNL KPEPIPIKTK VILIGTPEIY
YILYNYDEEF RKLFKIKADF DYEFEDNNEN MITFVKLIKY IVQEKNLKDI TFDGIQEISA
YAKRKAESKK YLTTNISSII EILEQANQIA KDNKNRYIDK NDIKLAIENK NKRNSLIKDK
ILSLYRQNKY IVDVTGFKIG QINALSVVDY GDFEFGRVNK VTVNTFCGNG NIINIDREVG
LSGNIFNKAI LILTGYIGEK FAQTGNLSFN ASICFEQMYG EIDGDSATLA ETVALLSSLA
EVPINQGIAI TGSVNQKGEV QAVGGVNTKI KGYFDICKIF GLDGSQGVII PESNVDDLVL
DDEILTAVKE GNFNIYTVNS VEDCFDILLP ASIKKGRKTN NFDYVEEKIL KRLNKFKDNK
EKQKKE
//
