ID A0A0B8P1M3_9VIBR Unreviewed; 352 AA.
AC A0A0B8P1M3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=JCM19231_2803 {ECO:0000313|EMBL:GAM57233.1};
OS Vibrio ishigakensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1481914 {ECO:0000313|EMBL:GAM57233.1, ECO:0000313|Proteomes:UP000031671};
RN [1] {ECO:0000313|EMBL:GAM57233.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RT "Vibrio sp. C1 JCM 19231 whole genome shotgun sequence.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAM57233.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RG NBRP consortium;
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RL Submitted (JAN-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 -!- 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:GAM57233.1}.
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DR EMBL; BBRZ01000048; GAM57233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B8P1M3; -.
DR Proteomes; UP000031671; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.
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 PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF56; LON PROTEASE; 1.
DR Pfam; PF05362; Lon_C; 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; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000313|EMBL:GAM57233.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000031671};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 161..342
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 352 AA; 38820 MW; 0881C394D591852C CRC64;
MRGDPSSALL EVLDPEQNNA FNDHYLEVDY DLSDVMFVAT SNSMNIPGPL LDRMEVIRLS
GYTEDEKLNI AKRHLLSKQI KRNGLKEHEI EVDDSAIIGI IRYYTREAGV RSLEREISKI
CRKAVKNILL DPKLKKVVVN EENLKEFLGV QRFDYGKADE SNRIGQVTGL AWTEVGGDLL
TIETESMVGK GKLTQTGSLG DVMQESIQAA MTVVRSRAEK LGINPDFYEK RDIHVHVPEG
ATPKDGPSAG IAMCTALVSS LTGNPVKADV AMTGEITLRG EVLPIGGLKE KLLAAHRGGI
KTVLIPKDNE RDLEEIPENV KKDIVVKPVQ WIDEVLTVAL QNDPSGVTLE TK
//
