ID G9YJA4_9FIRM Unreviewed; 198 AA.
AC G9YJA4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=HMPREF0080_01749 {ECO:0000313|EMBL:EHM38812.1};
OS Anaeroglobus geminatus F0357.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Anaeroglobus.
OX NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM38812.1, ECO:0000313|Proteomes:UP000005481};
RN [1] {ECO:0000313|EMBL:EHM38812.1, ECO:0000313|Proteomes:UP000005481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0357 {ECO:0000313|EMBL:EHM38812.1,
RC ECO:0000313|Proteomes:UP000005481};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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:EHM38812.1}.
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DR EMBL; AGCJ01000075; EHM38812.1; -; Genomic_DNA.
DR AlphaFoldDB; G9YJA4; -.
DR STRING; 861450.HMPREF0080_01749; -.
DR PATRIC; fig|861450.3.peg.1619; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_1375730_0_0_9; -.
DR Proteomes; UP000005481; 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; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
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:SF64; LON PROTEASE; 1.
DR Pfam; PF05362; Lon_C; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000313|EMBL:EHM38812.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005481};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 24..198
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 198 AA; 20820 MW; 541C7936A3783673 CRC64;
MELAKHVVQI GRFIPYATEK ASDKPAVGKV FGLGVAGYLG SVIEIEAVAF SARNEGKGYF
RFNDTAGSMA KDSLFNAAAV VRAVTGKELS DYDVNINFIG GGQIDGPSAG TAVTVALISA
ITGKPVRQDI AVTGEISVSG KVRAVGGIFE KAYGAARAGM KDMIIPAENK DDITEHHLNM
HIHAVTTIEE VLKLLTVD
//
