ID C7LPZ7_DESBD Unreviewed; 806 AA.
AC C7LPZ7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=Dbac_3407 {ECO:0000313|EMBL:ACU91479.1};
OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378 / X)
OS (Desulfovibrio baculatus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfomicrobiaceae; Desulfomicrobium.
OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU91479.1, ECO:0000313|Proteomes:UP000002216};
RN [1] {ECO:0000313|EMBL:ACU91479.1, ECO:0000313|Proteomes:UP000002216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4028 / VKM B-1378 / X {ECO:0000313|Proteomes:UP000002216};
RX PubMed=21304634; DOI=10.4056/sigs.13134;
RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., Del Rio T.G.,
RA Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Meincke L.,
RA Sims D., Brettin T., Detter J.C., Han C., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Desulfomicrobium baculatum type strain (X).";
RL Stand. Genomic Sci. 1:29-37(2009).
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; CP001629; ACU91479.1; -; Genomic_DNA.
DR RefSeq; WP_015775566.1; NC_013173.1.
DR AlphaFoldDB; C7LPZ7; -.
DR STRING; 525897.Dbac_3407; -.
DR KEGG; dba:Dbac_3407; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_0_1_7; -.
DR Proteomes; UP000002216; 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:UP000002216};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 567..762
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 226..253
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 657
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 700
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 806 AA; 89726 MW; A4541FDDECCDF5B2 CRC64;
MSKSLRLTPD QLRWTLDTST LPFETTDELE PLDEILGQDR GVDALRFGIG IHRPGYNILV
TGSPRTGRMD AVKKVLAKVV QDGKTPGDLC YLNNFKEPDA PILVRLGPGL GARLKKNMQQ
LVEELKKEVP KLFESSEYLA RKNEINEVYE KKTASFFMNL EKQVKEAGFA LVTFQGRQGQ
PPEVMPVVDG DPTPILKLEQ MVEKGRFPRE EFDRIKAKHL EIKTEIDSIF LQIRVLQKEI
QEKNRQADKL MFSNLAGDLI APLKADFACA ELDGYFQHMI DDMVDNIAIF FTQEHPPQLP
MGDPFEQYSV NVLVDNGEQQ GPPVIIEEYP TYRNLFGSIE RIVDRSGVWR TDFSRIKAGS
FVRANGGYLV LNLLDAIMEP GVWQSLKRAL KSRKMEIQTY DPFYLFTTSS MKPEPIEMDI
KVIVLADTYL YHMLQHYDDD VSKIFKVRAD FDSTMDKTGE SVLRFARFVR TQVAEHGLRP
FDRSAVAALV EEAVRMGGRQ EKMAATFPKL TDLLMEADYF AGQEGRDTVL HGDVSQAIET
RIHRSSLIEE KIQDMIDRGS IMIDTDGAKV GQINGLAVYN MGDVMFGKPS RITAATSMGK
AGIINIEREA ELSGSTHNKG VLILGGYLRK MFAQDKPLAV SASIAFEQSY SGVDGDSASS
TEMYALLSSL AGVPIKQGIA VTGSVNQNGE VQAIGGVNHK IEGFFACCKA KGLTGTQGVI
IPRANVLDLM LKTEVVEAVR EGRFNIWPVS SIEEGIELLT GKKAGTQKKD GTYPKGSIYA
LVDQRLKDLA EGMIKFGKED GKQEKA
//
