ID A0A1M5AT16_9BACE Unreviewed; 454 AA.
AC A0A1M5AT16;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Subtilase family protein {ECO:0000313|EMBL:SHF33391.1};
GN ORFNames=SAMN05444349_11662 {ECO:0000313|EMBL:SHF33391.1};
OS Bacteroides faecichinchillae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871325 {ECO:0000313|EMBL:SHF33391.1, ECO:0000313|Proteomes:UP000184436};
RN [1] {ECO:0000313|EMBL:SHF33391.1, ECO:0000313|Proteomes:UP000184436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26883 {ECO:0000313|EMBL:SHF33391.1,
RC ECO:0000313|Proteomes:UP000184436};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; FQVD01000016; SHF33391.1; -; Genomic_DNA.
DR RefSeq; WP_025075928.1; NZ_SSTN01000037.1.
DR AlphaFoldDB; A0A1M5AT16; -.
DR STRING; 871325.SAMN05444349_11662; -.
DR OrthoDB; 9792152at2; -.
DR Proteomes; UP000184436; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07493; Peptidases_S8_9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR017317; Pept_S8_subtilisin_bacteroid-2.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
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 PIRSF; PIRSF037903; Subtilisin_rel_GFO_2223; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 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}; Reference proteome {ECO:0000313|Proteomes:UP000184436};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..454
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030031261"
FT DOMAIN 169..438
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 392
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 454 AA; 50201 MW; 38382F548B0207E6 CRC64;
MKKFVLLAFA LNMVLGASAQ FTSTDTLKYR ISLKDKKTTT YSVKKPEMFL SKKSIERRKK
QGLSVNVTDL PVCKKYIDAI REKGVHILVT GKWDNFVTVS CNDSTLIDEI AKLPFVRSTE
RVWKGQAKKS QRRDSLINKP LRTDSLYGPA ITQIQMSNAN RLHEAGFKGQ GMTIAVIDAG
FHNADKIEAM NNIRILGTRD FVNPEADIYA ESSHGMCVLS CMAMNQPNVM IGTAPEASYW
LLRSEDEYSE NLVEQDYWAA AIEFADSVGV DIVNTSLGYY TFDDPTKNYR YRDLNGHYAL
MSREAGMAAD KGMVVVCSAG NSGMDSWKKT TPPGDAENVI TVGAIDKKGL LAPFSSIGNT
ADGRVKPDVV AVGLWADVMG TDGNLRHANG TSFSSPIMCG MVACLWQACP KLTAKEIIEL
VRHSGDRADF PDNIYGYGIP DLWKAYQSTI KKKR
//
