ID A0A495JIH5_9ACTN Unreviewed; 1464 AA.
AC A0A495JIH5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Subtilisin family serine protease {ECO:0000313|EMBL:RKR88826.1};
GN ORFNames=BDK92_3157 {ECO:0000313|EMBL:RKR88826.1};
OS Micromonospora pisi.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR88826.1, ECO:0000313|Proteomes:UP000277671};
RN [1] {ECO:0000313|EMBL:RKR88826.1, ECO:0000313|Proteomes:UP000277671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR88826.1,
RC ECO:0000313|Proteomes:UP000277671};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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:RKR88826.1}.
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DR EMBL; RBKT01000001; RKR88826.1; -; Genomic_DNA.
DR OrthoDB; 9813435at2; -.
DR Proteomes; UP000277671; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07481; Peptidases_S8_BacillopeptidaseF-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 3.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR033857; Bacillopeptidase_F.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR NCBIfam; NF038128; choice_anch_J; 1.
DR PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF01344; Kelch_1; 4.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00612; Kelch; 5.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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:UP000277671};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1464
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019775066"
FT DOMAIN 185..453
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 415
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1464 AA; 149635 MW; E8D1441587259943 CRC64;
MSHRPGSRSR LWRSFAIVSA VVLGITAQPA LAVAAPAAGA AVDPQVLREL STNGSTNFTV
YLREKANLST AASIGDADAR AAKVYEQLTG TATRTQRDLR AELDDRKASY KAFWIANALQ
VTSGNQALVN AIAARPEVER IAPTRTYELV KPTKAEPSGP GTSAVEWSVE NIQAPRVWNE
LGVRGETVVV ANIDTGAQYD HPALVGKYRG NLGGGNFDHN YNFFDPANIC AGDTPCDNNG
HGTHTMGTMV GDDGGDNQIG VAPGAKWIAA KGCETTGCSE ASLLASGQWV LAPTDSNGQN
PRPDLRPDIV NNSWGGGRGD PWYEETVAAW RAAGIFPAFA SGNTLGGAPC GSASSPGDNL
PSYAVGAYDI NNVIGDFSNR GPTVDGRTKP DIAAPGVNVR SSIPGGGYDS WDGTSMATPH
LSGAVALIWS AAPAIRGDVT ATEALLDETA TDTEALACGG TVDDNNIFGE GRLNAYEAVF
NAPRGGAGEV TGTVAEADGG EPIAGATVSV GSRTATTGTD GKYTLRLPVG DATLTIAAFG
FHTQTATVTV PDGTSVTKDF ALVGAQLVTV SGKVSDGSGH GWPLYAKIEV AGRPGGPVFT
DPFTGRYSFT VPGNATYAVT TTAKSAGYAP VSSELALEGA AKTLDVAVPV AAACQAPGYS
ANLGAPLLSE SFDTEETPEG WTLVNRTDDG GWEFDDPGNR GNQTGGSGNF AIIDSDILGV
GNTQDADLRT PTLNLTGVAA PVLKFNSDWR SVGSDSADID VSTDGGTTWA NVWHQTANLR
GPRVEEVPLT GLAGAATAQV RFRFNGSFAW WWQVDNVQVV NRICTPLPGG LVAGFTTDSN
TGAPLNGVTV TSGDVPADKG VSAATADDPN IGDGFYSFFS SVTGTHPFTA TKSPYRAVTK
NIAVAADNVR RGDFALKAGR LSVSPPQVES HQPYGSTRSA KVTVTNTGNA PAEVEVLERD
GTFDLLSQRG AALNEYEVKG LSTAQNGVAY GLAGNSAAAA PAIDPAWTRV ANTPAAVFDN
AAAVIDGKVY SVGGGTSSGN EKKTWVLDPE TNAWSTLADM PTARSKASAA AVGGKLYVIG
GWSASGAPVA SVDVFDPATG AWSTLAGATN PAPRAAAGTA IVDGKVYLVG GCADGSCTST
KNTVIFDPAS GTFSAGADYP IAVGWMSCGG IGGAVYCGGG AAGTTTFTDA FAYDPAGNAW
SALPDMPIDL WGAQYAAAGG LLVIAGGVTA NSSTVTNRSI AFDPATGEWQ NLPNAAFTRY
RGAGACGAYK VGGSPSSFVG SVETEYLGGL ELCDESGGDV SWLSTAPGTF TLAPGASKQV
TVTLTATAEA GVLQPGAYTA ELGLGSDTPY PVAAVPVEMN VSPPSGWGKV QGTVLGESCS
GTDVPVKATV RANLNGNPDT GYTLSSDSAG VYGLWLPKGK YDLIVAKDGW IPEVQRITVS
AGFVSTINFN LDPVTPCDTR VGGI
//
