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Database: UniProt
Entry: A0A0S2TD66_9GAMM
LinkDB: A0A0S2TD66_9GAMM
Original site: A0A0S2TD66_9GAMM 
ID   A0A0S2TD66_9GAMM        Unreviewed;       811 AA.
AC   A0A0S2TD66;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=Tel_07890 {ECO:0000313|EMBL:ALP53082.1};
OS   Candidatus Tenderia electrophaga.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Tenderia.
OX   NCBI_TaxID=1748243 {ECO:0000313|EMBL:ALP53082.1, ECO:0000313|Proteomes:UP000055136};
RN   [1] {ECO:0000313|EMBL:ALP53082.1, ECO:0000313|Proteomes:UP000055136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRL1 {ECO:0000313|EMBL:ALP53082.1};
RA   Eddie B.J., Malanoski A.P., Wang Z., Hall R.J., Oh S.D., Heiner C., Lin B.,
RA   Strycharz-Glaven S.M.;
RT   "Description of Candidatus Tenderia electrophaga gen. nov, sp. nov., an
RT   Uncultivated Electroautotroph from a Biocathode Enrichment.";
RL   Submitted (OCT-2015) 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}.
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DR   EMBL; CP013099; ALP53082.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S2TD66; -.
DR   STRING; 1748243.Tel_07890; -.
DR   KEGG; tee:Tel_07890; -.
DR   Proteomes; UP000055136; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000055136};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          564..759
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          135..166
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        654
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        697
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   811 AA;  89742 MW;  8991828CBABB5628 CRC64;
     MSNIKPLQAQ ALFQACDPSQ FDFDSTAELD DLSEVIGQAR ALEAIHFGMG IKKKGYNIFA
     LGPAGTGKHN VVTHLLKQQA SSEAAPCDWC YVNNFDAPHK PIALGLPPGT GRKLHDDMKQ
     LVEELRAAIP ALFEGDEYRA SIHELEEELK NQQERAIDEV RQAAQQKSIA LIRTPNGFAF
     APARDDEVID PKEFKKLPDD VKHKFEAEIA ELQEALEHIL RMAPQWRREA RERIKQLNAE
     LAMSAVGHLI DELREHYQDQ DEVLKYLDSV QEDVIANVDD FRRGEEEDAQ VVIGPNHSGG
     SFRRYQVNVL VDHSDSQGAP VVYEDNPTYQ NLIGRVEHMA MMGALITDFT LIKPGALHRA
     NNGYLVLEVY KLFQHPFSWE AIKRTLRSGE ICIGSLEQML SLVSTVSLEP EPVPLNVKVV
     LVGDRMLYYL LYQLDPEFQE LFKVAADFDD QMERSTESQQ LYAHLIATLA KKDKLRPFDR
     SGVARVIEHS ARVSENAAKL TTHMRSICDL LCEADYWADQ HGRELVNAED VQAAISAQIH
     RGSRMKERLH EHIQRGILLI DSSGTAAGQV NGLSVIDLGN ISFGVPTRIT ARVRMGDGDV
     LDIEREVDLG GPLHSKGVLI LAGFLGARFA KECPLALSAS LVFEQSYGEI EGDSASSAEL
     YALLSALSGV PIKQGFAVTG SVNQHGQVQA IGGVNEKIEG FFDVCSERGL NGEQGVLIPP
     SNVGDLMLRR DVIAAAEQGK FHIYAVETID QGIELLTGVP AGVPDAEGNY PHGSINHKVA
     QQLLKFAEIR HEFGDLKKDH DDGAHHDKDD D
//
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