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Database: UniProt
Entry: W7Z6R2_9BACL
LinkDB: W7Z6R2_9BACL
Original site: W7Z6R2_9BACL 
ID   W7Z6R2_9BACL            Unreviewed;       441 AA.
AC   W7Z6R2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=JCM16418_4184 {ECO:0000313|EMBL:GAF10014.1};
OS   Paenibacillus pini JCM 16418.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF10014.1, ECO:0000313|Proteomes:UP000019364};
RN   [1] {ECO:0000313|EMBL:GAF10014.1, ECO:0000313|Proteomes:UP000019364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF10014.1,
RC   ECO:0000313|Proteomes:UP000019364};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from the
RT   Rhizosphere of Pine Tree.";
RL   Genome Announc. 2:e00210-14(2014).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:GAF10014.1}.
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DR   EMBL; BAVZ01000017; GAF10014.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7Z6R2; -.
DR   STRING; 1236976.JCM16418_4184; -.
DR   eggNOG; COG0466; Bacteria.
DR   Proteomes; UP000019364; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; 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   CDD; cd19500; RecA-like_Lon; 1.
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; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR004815; Lon_bac/euk-typ.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00763; lon; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF56; LON PROTEASE; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 1.
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; PS01046; LON_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000019364};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}.
FT   DOMAIN          255..436
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        342
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   441 AA;  48694 MW;  DF6109856D36A0CF CRC64;
     MAVQKLVKKM KGPILCLVGP PGVGKTSLAR SIARSLNRKF VRISLGGVRD EAEIRGHRRT
     YVGAMPGRII QGMKTAGAAN PVFLLDEIDK MASDFRGDPS SALLEVLDPE QNNTFSDHFI
     EVPFDLSQVM FVTTANAIHN IPRPLLDRME VLNIPGYTEL EKLQIAKRYL LPKQKREHGL
     QEEQLHIGEE ALFKVIREYT RESGVRNLEQ QVAALCRKTA RRIVSEEQET IEIGPEDIKE
     YLGSAKFRHS VADLEDQIGT VTGLAWTEVG GETLMIEVTV VPGTGKLILT GQLGDVMKES
     AQAAFSYTRS KSVDLGIDSD FHEKNDIHIH IPEGAIPKDG PSAGITIATA LISALSKKHV
     SKHVAMTGEI TLRGRVLPIG GLKEKSLAAH RAGYKKILLP KDNERDLRDI PDSVKEDVEF
     VPVSHMDQVL KHALVEQTEV H
//
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