ID A0A1I6F7W4_9PSEU Unreviewed; 510 AA.
AC A0A1I6F7W4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Serine protease, subtilisin family {ECO:0000313|EMBL:SFR26054.1};
GN ORFNames=SAMN04488564_109205 {ECO:0000313|EMBL:SFR26054.1};
OS Lentzea waywayandensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=84724 {ECO:0000313|EMBL:SFR26054.1, ECO:0000313|Proteomes:UP000198583};
RN [1] {ECO:0000313|EMBL:SFR26054.1, ECO:0000313|Proteomes:UP000198583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44232 {ECO:0000313|EMBL:SFR26054.1,
RC ECO:0000313|Proteomes:UP000198583};
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}.
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DR EMBL; FOYL01000009; SFR26054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6F7W4; -.
DR STRING; 84724.SAMN04488564_109205; -.
DR OrthoDB; 9766923at2; -.
DR Proteomes; UP000198583; 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; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
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 InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..510
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011688139"
FT DOMAIN 390..510
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 181
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 510 AA; 51576 MW; A806E5E19C8CE252 CRC64;
MHRTTCGLAV LIVASALLAT PAQAAEADFV KARNPAAGGS FIVSLKPGAA IQSTSSALTQ
KYGGDLDAVF SHAMRGFQVK NLTEAAARKL AADPAVKAVY QDGTAKALDV QDNPTWGLDR
VDQASLPLDK KFNYPSGGAS NVTVYITDTG VKTSIADFEG RASVGADFIE DGQNGQDCSG
HGTHVAGTVG SKTYGVAKKA KLVSVRMLGT SCTGNGPDSA GVKAIEWITA NAKKPAVVNA
SWTFDTADIG NDAIAGMVAS GVQMAVASGN SSTDACSTGP AKIASLITVN ATSSNDARAS
FSNYGTCTDI FAPGDNITSL GLNGGSTNMS GTSMATPHVA GVAALYLSAN PSASPQALRD
ALVNNATSGK VTNPGSGSPN KLLYSGFIGG GPDPQCGPGT NGDDVSIPDT GTAVSSSVTI
SGCTGNSTAS ATVKVDINHT YTGDLAVDLV SPSGRTYVLK KAGGASSSGG IHETYTVDLS
SEARNGTWKL QVKDIYTYDV GNIDTWTLTV
//