ID W7YB83_9BACT Unreviewed; 287 AA.
AC W7YB83;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=JCM21142_259 {ECO:0000313|EMBL:GAF01646.1};
OS Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Saccharicrinis.
OX NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF01646.1, ECO:0000313|Proteomes:UP000019402};
RN [1] {ECO:0000313|EMBL:GAF01646.1, ECO:0000313|Proteomes:UP000019402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF01646.1,
RC ECO:0000313|Proteomes:UP000019402};
RA Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA Iida T., Darby A., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT Anaerobe Isolated from Marine Mud.";
RL Genome Announc. 2:e00206-14(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 -!- 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:GAF01646.1}.
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DR EMBL; BAMD01000002; GAF01646.1; -; Genomic_DNA.
DR AlphaFoldDB; W7YB83; -.
DR eggNOG; COG0466; Bacteria.
DR Proteomes; UP000019402; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 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:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 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 Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000019402};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 107..287
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 287 AA; 31593 MW; A0AF5F97D81D8913 CRC64;
MELIEVSGYI LDEKTEIAKR HLWPNQLENH GIAKSKVSLS KKVMAFVIEN YTRESGVREL
NKVLAKLARK YALKIATNKE FKKTISVDDI KENLGVQRFS KEKWQDTHVP GVVTGLAWTA
VGGEILYIES SLSKGNGKLT LTGNLGDVMK ESAVLALEYI KSNCKVFGIE AKMFEENNIH
VHVPEGAIPK DGPSAGITMA TALVSSFSGK KVKKRIAMTG EITLRGKVLP VGGIKEKILA
AKRAGIKEII LSKDNMKDVG EIKDVYVEGL EFHYVNSIKE VLDVAIV
//
