ID A8LB72_FRASN Unreviewed; 491 AA.
AC A8LB72;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ABW09533.1};
GN ORFNames=Franean1_0066 {ECO:0000313|EMBL:ABW09533.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09533.1};
RN [1] {ECO:0000313|EMBL:ABW09533.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW09533.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT "Complete sequence of Frankia sp. EAN1pec.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP000820; ABW09533.1; -; Genomic_DNA.
DR AlphaFoldDB; A8LB72; -.
DR STRING; 298653.Franean1_0066; -.
DR KEGG; fre:Franean1_0066; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_031617_0_0_11; -.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00306; Peptidases_S8_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF7; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-1 PROTEASE; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 165..471
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 60..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 418
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 491 AA; 52731 MW; 0971BF2345955452 CRC64;
MPLGGSMGGL GVVDVMVKMQ PSDGGSVADS LDQADEVMRS ADITLDSHFE PIRMQGKSRV
GRDEILPYGG DRFRPSSSAG EDAELRTEKG GPACVIVRAS VDTCDPREIE GSLIELNRRS
EVISIYSDPE IAPYWKCWRE NQPENLSDML SVLNLQELSA VGMDGDGVDV AVVDGGIDAD
YLVQRSRDLK PLEGWHPDNL QNTPGQYAVN NDRDAAHGTM CAHEVLLASP RARILDYALL
RRAATVNNKA TMSGLDIRFS HAIAAYHALA SRLRKDRRSN GGSLSRPLVV TNSWGLGSVA
SDEVTNRLGR YRDQFEHPFN LAVEELSLAG ADIVFAAGNN GQPHPDDSTW PQDELPITGA
NSHPLALCVG AVTVGGERIC YSSQGPGRLF WGKPDVMGYS EYVGSEVLGS DTPDVGTSAA
CPLVAGVIAA VRSKIGTDVL SPVKLREAVR CSAWMPSVAG HCKPNSEYGW GIIDPSALLA
GVREHLTQSR E
//
