ID A0A223NSJ7_9SPHI Unreviewed; 550 AA.
AC A0A223NSJ7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=MuYL_0728 {ECO:0000313|EMBL:ASU32628.1};
OS Mucilaginibacter xinganensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1234841 {ECO:0000313|EMBL:ASU32628.1, ECO:0000313|Proteomes:UP000215002};
RN [1] {ECO:0000313|EMBL:ASU32628.1, ECO:0000313|Proteomes:UP000215002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJC16-A31 {ECO:0000313|EMBL:ASU32628.1,
RC ECO:0000313|Proteomes:UP000215002};
RG Henan University of Science and Technology;
RA You X.;
RT "Complete genome sequence of Mucilaginibacter sp. strain BJC16-A31.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CP022743; ASU32628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223NSJ7; -.
DR KEGG; muc:MuYL_0728; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000215002; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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:UP000215002};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..550
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012488452"
FT DOMAIN 67..506
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 465
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 550 AA; 59507 MW; 1CF8C20F1F51E4D2 CRC64;
MHKLRKYALS SLVCGAMFLS LNAIGQQIPK QAPDPPKNWH TLDLKADGFY GISLKPAYLF
LKGKKSKTVI VTTIDSGIDT LQNDLKSILW VNPKEIPNNG IDDDKDGYVD DVHGWDFLGG
KGGKVDFTET TEEVRLYHKL KGKYAAVTTA PAGQEKEFAF WQSVKTNYDS TMSKSQAEVK
DLTMEVNVLT ATNYYIKREL KLKSDQTFTL GDLKKINTTN DTINQSKTVW ESVFSQIGDD
ANNAKVLKDL TEYFAKQNNN ISPDLDARAR IVGDDPDVND GKPYGNNILK NADASHGTGV
AGLIGAVRNN GYGIDGVADN VRIMSIKAVP NGDEYDKDIA NAIRFAVDHG AQIINMSFGK
KISPHKDWVD AAFKYAAQKD VLLVMASGND GQDVDAKPEF PNDTYLDGST TDNVINVGAS
GPKADTALAA TFSNYGKNNV DVFAPGVKVT SIDTDAEFNT ADGTSFASPI VAGVAALCLE
YYPGLSAKQL KQVIMESATP VTGKKVNKPG AKEKVDFTSL SKTGGIVNAY KALEIASKMK
GERQLATGSF
//
