ID   A0A1H9UMG9_9BACI        Unreviewed;       588 AA.
AC   A0A1H9UMG9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Fervidolysin. Serine peptidase. MEROPS family S08A {ECO:0000313|EMBL:SES10327.1};
GN   ORFNames=SAMN04487944_11843 {ECO:0000313|EMBL:SES10327.1};
OS   Gracilibacillus ureilyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=531814 {ECO:0000313|EMBL:SES10327.1, ECO:0000313|Proteomes:UP000199687};
RN   [1] {ECO:0000313|EMBL:SES10327.1, ECO:0000313|Proteomes:UP000199687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7727 {ECO:0000313|EMBL:SES10327.1,
RC   ECO:0000313|Proteomes:UP000199687};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOGL01000018; SES10327.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9UMG9; -.
DR   STRING; 531814.SAMN04487944_11843; -.
DR   Proteomes; UP000199687; 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   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR032812; SbsA_Ig.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF13205; Big_5; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00635; BID_2; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 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:UP000199687};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..588
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011640488"
FT   DOMAIN          401..478
FT                   /note="BIG2"
FT                   /evidence="ECO:0000259|SMART:SM00635"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        183
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        339
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   588 AA;  65013 MW;  CADAA179519516A9 CRC64;
     MRKLLSIITA LSLLLVVLNS QSVFASENHT IDKMLKENIL KERKENEILI QYKQETNNNS
     SKIQLLSQSD SVETVELNDY VDQKKIINQL EQMEDVQFVE ENKKVYVQST TIISDPYYEL
     QWALDKVAAP EAWEVLTEPG EEVVVGVIDT GVDLQHEDLQ GKILQNGYNF IDESEAVYDM
     NGHGTAVSGV IAASINNDLG IAGVTGKSNV KILPLQAGFS DGSLYLSDIV EAIDYAIEQN
     VDVLNLSFGS PDFSNIEYNA IQRAVDNGII VVASAGNNGN SEYMYPASYH NVISVGSIDQ
     YNNLSNFSTY NDKVDIVAPG EEIVTTTKNN QYTYQNGTSF SAPIVSGIIA SIISEKQNVT
     LNEIMPAIQE TSVDLGPAGK DEKFGYGLID FYQLSQKMFP EIEQIIIEQP QVELTVGETL
     KIQPIILPTE AASNQLFWES SNNEVVTVNE EGVINGVTTG KATISISSAD SSVTSFVEVN
     VVDKELIENE TFEPIYNAAL DQEWAINFNN SVDATSINNQ TVQIIDSSNN QLPLEFSFTN
     QHKTVKVKSL ELYEPNSTYK LVISKDICSQ DGKSCLSKPV YQVFHTRE
//