ID A0A1B9NIZ6_9MICO Unreviewed; 1001 AA.
AC A0A1B9NIZ6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Serine protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=A7J15_11185 {ECO:0000313|EMBL:OCG76540.1};
OS Microbacterium sediminis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=904291 {ECO:0000313|EMBL:OCG76540.1, ECO:0000313|Proteomes:UP000093355};
RN [1] {ECO:0000313|EMBL:OCG76540.1, ECO:0000313|Proteomes:UP000093355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-01 {ECO:0000313|EMBL:OCG76540.1,
RC ECO:0000313|Proteomes:UP000093355};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCG76540.1}.
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DR EMBL; LXMD01000001; OCG76540.1; -; Genomic_DNA.
DR RefSeq; WP_067027987.1; NZ_KV744790.1.
DR AlphaFoldDB; A0A1B9NIZ6; -.
DR STRING; 904291.A7J15_11185; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000093355; 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; cd02120; PA_subtilisin_like; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 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; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
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 InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
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:UP000093355};
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..1001
FT /note="Serine protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008632083"
FT DOMAIN 45..145
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 176..660
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 436..524
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 705..796
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 185
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 607
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1001 AA; 102285 MW; D1BF2278B8FB1E4E CRC64;
MTRPLPRAAA ALTLALALTA TSALAGHAAV EEVKPIAPVT AEDGRYIVLF AEDALATYDG
GVPGIEATKP AKGNKLDAHT KNAQKYIEHL EKKQQQVADE IGVTPDTTYQ VTANGFAAEL
TAEQVATLRA DKTVLGVFPD EIRTVDAVPS TEFLGLGSAD GSGGVWEATG GVETAGEGIV
VGVVDTGIAP ENPSFAGEKL KKQKQTPAGE PYTTGTEIVF PKADGGEFRS TIVTGEEWDK
HDYSTKIIGA QWFGEGFEAV TDDDYLSPRD GDGHGSHTAS TAAGNFGVDA TVSGVDFGAI
TGVAPAAKIA AYKACWNGPD PSTTDDDGCA LSDLTAAIDT AVRDGVDVIN YSIGGGSATT
VLSPEDISFY NAAAAGVFVA VSAGNSGPGA ATADHASPWY TTVAASTIPT WEGTVELGDG
FTAPGVTVSV PDGQTVTGDV VYAGDIPAAG AAASDAALCL LGSVDDAAAA GKIVICDRGS
NARVEKSQEV AESGGIGAIL TNVAPGESLD NDFHSVPTVH VAAEYRAAIV AYSRDAAAPV
ATLHSDNITD VVTPTPQVAG FSSRGPMNAE TNDVIKPDVS APGVAILAAT TNGSKEAPTW
GILSGTSMAS PHVAGLGALY LGEHPTMAPA DIKSALMTTA YDTVNGDGSP NTDPFAQGAG
HVDPTKMFEP SLVYSSGPID WAGYLQGLGL ANFGLPEEDL VAPSDLNLAS IGIGSLSAPE
TITRTITATE AGTYTATAEV PGIDVTVEPS TVTLADGESA TFTVTFAKAD APAEQWTTGF
LTWTGGTNDV RSPIAVYPVT ATAPAEVTGT GTEGSLEVGI TSGVTGDLAL HTAGLAKAER
LIDGDETTGA AEDGHSYALV TVPEGADLAR FVQDSSDDAA SDLDLFVYRV VSDTDWRYYE
MWQSATGSAD EEVVRTAPTA GTYLVEAHVY AYEDPFTWTL DAAVASPGEG LEAAPNPLPV
VNGQDATFNV RWSGLEPGAT YSGSVRYGDS SIRTLVTVTA E
//
