ID A0A098EL51_9BACL Unreviewed; 726 AA.
AC A0A098EL51;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Subtilisin NAT {ECO:0000313|EMBL:CEG22001.1};
GN Name=aprN {ECO:0000313|EMBL:CEG22001.1};
GN ORFNames=BN1080_00921 {ECO:0000313|EMBL:CEG22001.1};
OS Planococcus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1499687 {ECO:0000313|EMBL:CEG22001.1, ECO:0000313|Proteomes:UP000043699};
RN [1] {ECO:0000313|EMBL:CEG22001.1, ECO:0000313|Proteomes:UP000043699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES2 {ECO:0000313|EMBL:CEG22001.1,
RC ECO:0000313|Proteomes:UP000043699};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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; CCXS01000001; CEG22001.1; -; Genomic_DNA.
DR RefSeq; WP_052650740.1; NZ_LR698965.1.
DR AlphaFoldDB; A0A098EL51; -.
DR STRING; 1499687.BN1080_00921; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000043699; 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; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 2.60.40.1080; -; 2.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 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; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR001119; SLH_dom.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF00395; SLH; 3.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00635; BID_2; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 2.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51272; SLH; 2.
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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000043699};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 555..613
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 614..677
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 314
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 726 AA; 75775 MW; 028436806FEDFC94 CRC64;
MKVIGSGFMA LALLVFGADE IPASAQGEKE QKMIVVFEEQ ADMEEIIEDA GGTATEAFEE
VDIASAELTD SVINELRQDP AILSIEEDTV VELQAQMEDW GIASSNIPAA WNSGFTGEGI
KISVIDSGIS RHEDLKLAGG ISTVDYTNSY ADDQGHGTHV AGIIGGLNNS YGVKGVAYDA
ELYAVKAFDA KGQAYVSDMI EGINWSVAND MDIINLSAGS QTGSTAFKSA ADKAYASGLL
IVAAAGNDGD SVGAGDTVDF PARYPSVIAV GAVDRSSKRA DFSSTGSTVE VTAPGERILS
TYTGNQYAYL SGTSMATPYV AGELALIKQA YPNLTNKELR QVLIDHTRDA GPAGKDPYYG
YGIIRASSFT APPRSQQVNA VANLALNSKA ITGAPGDMFS LSATATFQDG SVQNVTPDAV
WASADVKVAT VANGKVQLKA YGSTTITATF GGKSATATIT VPQPEANPVV KLEADQTTLV
GKPGDVFTVS AAATFKNNQK EMVTNEAVWT SSNEAIATVS NGKITVQGYG MATVSLSFGG
QTATVIVNSP NPQAAPNKIH FDDVPSFYAP AVDYLVQRGI TQGKSATQFG VTDSIIRADA
AVWLAKELGL NTATARPSGF GDVPDRAAGA VNALKQAGII GGKTATRFGS YDPLTRGEVA
IILQRTYKLD AGNETSAFTD VSSRYADAVN ALVANDVTDG LTPKQFGVSR NITRGQLAVF
IYRLAE
//
