ID D1C8E0_SPHTD Unreviewed; 816 AA.
AC D1C8E0;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=Sthe_2669 {ECO:0000313|EMBL:ACZ40083.1};
OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales;
OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ40083.1, ECO:0000313|Proteomes:UP000002027};
RN [1] {ECO:0000313|Proteomes:UP000002027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC {ECO:0000313|Proteomes:UP000002027};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R.,
RA Goeker M., Klenk H.P., Eisen J.A.;
RT "The complete chromosome 2 of Sphaerobacter thermophilus DSM 20745.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ40083.1, ECO:0000313|Proteomes:UP000002027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC {ECO:0000313|Proteomes:UP000002027};
RX PubMed=21304676;
RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Desulfohalobium retbaense type strain
RT (HR(100)).";
RL Stand. Genomic Sci. 2:38-48(2010).
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 ---------------------------------------------------------------------------
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; CP001824; ACZ40083.1; -; Genomic_DNA.
DR RefSeq; WP_012873121.1; NC_013524.1.
DR AlphaFoldDB; D1C8E0; -.
DR KEGG; sti:Sthe_2669; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_0_1_0; -.
DR InParanoid; D1C8E0; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000002027; Chromosome 2.
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:UP000002027};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 568..763
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 138..169
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 212..243
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 658
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 701
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 816 AA; 91533 MW; 26F0C269C1CBDF59 CRC64;
MESIRERLAV PPERLRRRLD PASLPFKTTA EVEPLNGTIG QPRALDAIEF GLDVQNHGYN
LYVAGVPGSG RETTVRDYLG RYARTRPTPS DWIYVHNFDE ADRPNAIPLP AGRGVQFARE
MDEFLESARQ EIPRAFDSED YERRRREALA ELGQRREELF RQMNEFAANR GFVLEATPTG
ILSIPVVQGR PLSPEEFERL PAEVQQEIRN RDAEIQEHVS RALRQVRQLE KEAAERVRKL
DRDVVTFLVG PMLDDLRDRY QDCPEVVAYL EAVRNDLPEH IDMFRQARQP AVALPIPQPA
QAQPDLNRYR VNVLIDNSHL DGAPVVIERN PSYYNLIGRI DYRATFGAMV TDFRQIRPGA
LHRANGGFLV LHVVELLREP FAWDALKRAL VTRSIQIENL GEQYSAVPMA RLRPEPIPLS
VKVVLIGPLE VYHILYQIDE DFQELFKVRA DFGPDMDWID EHVQNYAAFI SRRVHEWGLR
HFDRSAVARV VEYGARQREH QGKLSTRLLD IANIVAEASY WAEKAGHEFV QADDVDQAIR
KRRYRSNLVE ERIRELLTDG TIMIDVDGEA VARVNGLAVL SFGDYAFGKP SRVTARVSAG
RGSIVSIERE IELSGPIHSK GVMILSGYLR GHYGQHVPLA ITATLTFEQS YEGVDGDSAS
STELYALLSA LSGLPLDQGI AVTGSVNQFG EVQAVGGVNQ KIEGFYAVCK EKGLTGRQGV
IIPAANVKNL MLDDDVVEAV RAGRFHVWAV RTIDEGIEIL TGRPAGERGP DGQYPEGTVH
RLVEDRLRRY AEEVRAFAAP DGAAGAAQVA SGEESQ
//
