ID A9EJ70_9GAMM Unreviewed; 589 AA.
AC A9EJ70;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-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 ORFNames=KT99_13627 {ECO:0000313|EMBL:EDP99672.1};
OS Shewanella benthica KT99.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=314608 {ECO:0000313|EMBL:EDP99672.1, ECO:0000313|Proteomes:UP000005839};
RN [1] {ECO:0000313|EMBL:EDP99672.1, ECO:0000313|Proteomes:UP000005839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT99 {ECO:0000313|EMBL:EDP99672.1,
RC ECO:0000313|Proteomes:UP000005839};
RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP99672.1}.
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DR EMBL; ABIC01000034; EDP99672.1; -; Genomic_DNA.
DR RefSeq; WP_005501466.1; NZ_ABIC01000034.1.
DR AlphaFoldDB; A9EJ70; -.
DR MEROPS; S16.A10; -.
DR Proteomes; UP000005839; 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; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR041699; AAA_32.
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 PRINTS; PR00830; ENDOLAPTASE.
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}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 345..540
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 478
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 589 AA; 65510 MW; 19F8C55DC6C94BAE CRC64;
MNPNVIPVSS LTPQHNLPVL STLKNAKKNL LLGQERVVDA FTLLTKTAHQ HMYLADFAGI
DRKAFIDALA NQQENKAPQL LIGSNDSNTL SFQWIEQQEL VLDEEKEPLV FTHKRQNYSY
LSGNIKRTDL VGRLLNTRQH PVNADNLDKL QYQAGALAQC HTLFICADSL WKREGLWDLL
LNILSSKSYK IHSLLPPVPL NCKIVLVGTS NQYSACWIEE SQFSTHFPLL GEMSYELDLT
HHTEEEYGNW LISVAALNQV SLSQSALAPL FQYSARLADH QRRLTLLSSQ VGQLISQAHA
YCGKSEISAD DITYALTRYQ LRHNASETLS AQNFDDKFIN LPTDGERIGQ INGLTVLETV
EYCYGEPARI TASVHYGDGE VADIERKSEL GGNIHAKGMM ILSSCLYRIF GKNAPLHLNA
NIVFEQSYQE IDGDSASLAE YCSLISAITE KPINQSIAAT GAIDQFGQVQ AIGGVNEKIE
GFFNLCERRG LTGIQGVIIP RANTQQLNLS AKLVAAIKAE KFSIFQIKHI DEAIELLMNT
TAGVADEDNH FPEDSLYGLV QARLASLAGY SDEESTFFEK LLRKLKFSS
//
