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Database: UniProt
Entry: A4B9D3_9GAMM
LinkDB: A4B9D3_9GAMM
Original site: A4B9D3_9GAMM 
ID   A4B9D3_9GAMM            Unreviewed;       797 AA.
AC   A4B9D3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=MED297_20142 {ECO:0000313|EMBL:EAR11234.1};
OS   Reinekea blandensis MED297.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Reinekea.
OX   NCBI_TaxID=314283 {ECO:0000313|EMBL:EAR11234.1, ECO:0000313|Proteomes:UP000005953};
RN   [1] {ECO:0000313|EMBL:EAR11234.1, ECO:0000313|Proteomes:UP000005953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED297 {ECO:0000313|EMBL:EAR11234.1,
RC   ECO:0000313|Proteomes:UP000005953};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (FEB-2006) 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}.
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:EAR11234.1}.
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DR   EMBL; AAOE01000001; EAR11234.1; -; Genomic_DNA.
DR   RefSeq; WP_008044757.1; NZ_CH724151.1.
DR   AlphaFoldDB; A4B9D3; -.
DR   STRING; 314283.MED297_20142; -.
DR   HOGENOM; CLU_014785_0_1_6; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000005953; Unassembled WGS sequence.
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; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF49; LON PROTEASE HOMOLOG-RELATED; 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   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000005953};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          564..759
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        654
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        697
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   797 AA;  89507 MW;  0433FC222B57301F CRC64;
     MSTLPSPLAA SDLTAQIDLS HLNIESTADL DGVSSFLGQP RAKKSLEFGI AMRGSGYNLY
     VMGDSGTGRQ SLVSKYVRGL AESQQAPSEW AYINNFESPR EPSALEVPAG RGDVLKEQIQ
     QLVNDLMDTF PSAFENPTYQ RKRTMIDREF NQKYDMAIKL VERFANEKEV AVVADGGSVM
     LLPVIDGKAL DDTEFAQLPE QVRSEFQSRI NDIEEYLNEQ VLELPTWRRK SSEKLRQLNL
     ETVQQAIRPL IKELEVKNQS QLSILRYIRE VKNHLPQQIV DLFAEESMMD TRTDQDRRAA
     LEGWLKPNLM TQHEINDGAP VIYEMLPTYQ NLFGRIEYAT QQGIPITNYQ LIRPGSLLRA
     NGGYLILDAE KLLIEPYAWD ALKLALKTKE LKMESPYADA SLMHAVTLSP ESIRLNVKVV
     LLGSRDIYYQ LQEWDPEFME LFRVPVDFDS FIPSNRDNID NLILRIKDYG ETKGFKPLTK
     AALERLIEYS LREAEHQKRL SAQVAKVFKV FAEADYISRH KEARFIEASH VTEALEAADY
     RNSRIADQML QEIEEGTILI DTDGQRVGCV NGLTVMEIGE SCFGSPARIT ATVHVGGKGV
     VDIEREVELG QSIHSKGVMI LSGFLGHEFG RQFPLTLSSH IAMEQSYGYI DGDSATVAEY
     CSLLSAITQA PVNQHLAITG SMNQLGEVQA IGGVNEKIEG FFKLCQLRGL NGRQGVIIPA
     DNQKHLMLHQ SVIDAVEAGQ FHIYSVRHVY QALALLMDRE PGEVSDKGEF PESSLNGQAQ
     TALKKLFELY QETEEGE
//
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