ID F8A905_THEID Unreviewed; 805 AA.
AC F8A905;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=Thein_0170 {ECO:0000313|EMBL:AEH44055.1};
OS Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfatatoraceae; Thermodesulfatator.
OX NCBI_TaxID=667014 {ECO:0000313|EMBL:AEH44055.1, ECO:0000313|Proteomes:UP000006793};
RN [1] {ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders L.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermodesulfatator indicus DSM 15286.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEH44055.1, ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RX PubMed=22768359; DOI=10.4056/sigs.2665915;
RA Anderson I., Saunders E., Lapidus A., Nolan M., Lucas S., Tice H.,
RA Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Chang Y.J.,
RA Brambilla E.M., Rohde M., Spring S., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of the thermophilic sulfate-reducing ocean
RT bacterium Thermodesulfatator indicus type strain (CIR29812(T)).";
RL Stand. Genomic Sci. 6:155-164(2012).
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; CP002683; AEH44055.1; -; Genomic_DNA.
DR RefSeq; WP_013906802.1; NC_015681.1.
DR AlphaFoldDB; F8A905; -.
DR PaxDb; 667014-Thein_0170; -.
DR KEGG; tid:Thein_0170; -.
DR PATRIC; fig|667014.3.peg.176; -.
DR eggNOG; COG1067; Bacteria.
DR eggNOG; COG4980; Bacteria.
DR HOGENOM; CLU_014785_0_1_0; -.
DR InParanoid; F8A905; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000006793; Chromosome.
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:UP000006793};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 570..765
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 208..249
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 660
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 703
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 805 AA; 91317 MW; D4709DA6CE98DEBE CRC64;
MTVTVKTLKP EEVRLTVAPS DLKVTSFEEL LETLETEKPI MAQERAIRAL DFGLNFEDLD
FHMYVAGTPE LGTSYITRAL VESQARERPT PSDWCYVYNF KDPDVPKALE LPPGKGREFQ
KDMADLIETL RQKIPEAFES EAYITKKEQI IREFNVTRAK IFEELEQKVK AEGFILNVEP
FGMMIIPAKP DGTPMTPEDV KELPEEVKEN LKRKSEFLQK ELNATARRIQ QLEKDLRQKL
KELDREVALN VVGSFIQELR EKYATTKGVV SFLNEVQEDI IKHLDDFRQK PAPQPPMPFP
MPPAQPSFTR YEVNVFVDNS ECQGAPVIFE PNPTYTNLFG TIERKAQFGA LITDFTMLKA
GSLHKANGGF LIVRALDLLK YPFSWENLKR AIKTRKIYLE DLAEQIGLFT TKTLKPEPIP
FRAKVVLQGD PFIYHLLYIY DENFREVFKV KAHLDRWVDR TEETTRQFLQ AVAAMVKHNQ
LLPLENDALA KIVEYSCELA GRQDKLSLEL PVIQDVLKEA HFWAKREQKE AINAFHIEKA
INERKFRANL SEERLQEMIE KDIIKIQVDG ELCGSINGLS VYDLGDYSFG RPTRITANIS
LGKEGVVNIE READLSGKIH TKGVLILAGF LRERFVHDKP LTLTATLCFE QSYGLVDGDS
ASSAELFALI SALSGVPIYQ GIAVTGSVSQ KGDIQPVGGI NQKIEGFYKV CKAKGLNGKQ
GVIIPQANVK ELMLDKEVVK AIEEGQFHIW AISRVEEGIE ILTGKPAGER KPDGTYPEGT
IFYLVDQKLR ELAKLARDFA KEEKK
//
