ID   A0A1C4XI48_9ACTN        Unreviewed;      1470 AA.
AC   A0A1C4XI48;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Serine protease, subtilisin family {ECO:0000313|EMBL:SCF08094.1};
GN   ORFNames=GA0070607_5283 {ECO:0000313|EMBL:SCF08094.1};
OS   Micromonospora coriariae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=285665 {ECO:0000313|EMBL:SCF08094.1, ECO:0000313|Proteomes:UP000198243};
RN   [1] {ECO:0000313|EMBL:SCF08094.1, ECO:0000313|Proteomes:UP000198243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44875 {ECO:0000313|EMBL:SCF08094.1,
RC   ECO:0000313|Proteomes:UP000198243};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; LT607412; SCF08094.1; -; Genomic_DNA.
DR   OrthoDB; 9813435at2; -.
DR   Proteomes; UP000198243; Chromosome i.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 4.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR011628; Cleaved_adhesin.
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   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF07675; Cleaved_Adhesin; 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; 4.
DR   SUPFAM; SSF117281; Kelch motif; 1.
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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..1470
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008708070"
FT   DOMAIN          194..475
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          676..753
FT                   /note="Cleaved adhesin"
FT                   /evidence="ECO:0000259|Pfam:PF07675"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        249
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        419
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1470 AA;  151705 MW;  96CE4CBB0CA89CBA CRC64;
     MFRRPQWRRT ARSLVSAGAA MILAATCLAS IGSGAQAAPG GTGAGAAPGD KIRPELAKQL
     QAKSEGDFWI RFKDRADLSK ASAIKDWSKR GAAVAEALRR TAADSQGKIR AELDGSGTKY
     QTFWATNAIK VSSGSLAMVQ KFAAHSEVEG LYAPVAYKVP EVTKGTDEKT VNALEWGIAN
     INADDVWSQY GVTGEGITIA NIDTGVQFDH PALVGSYRGN NGDGTFDHNY NWYNAAGTCA
     TAPCDTNGHG THTMGTMAGS DGANQIGVAP GVKWIAANGC CPSDAALIES GQWMLEPLDL
     NGQNPDASKR PNIINNSWGS QNPSNEPFME DVTLAWAASG IFGVWSNGNS GPACQTSGSP
     GSLVSNYSTG AYDINNNVAG FSGRGVGQNG EIKPNISAPG VNVRSSIPGN AYGSISGTSM
     AAPHLAGAIA LLYSAAPSLV GDINATRALL NGAAIDKADD QCGGTPADNN VYGEGRLDAL
     ALLNAAPTGD TGTLAGTVTD AATGSPIAGA TLTLTGPTGR EVTTGADGKY STTLPIGDYQ
     VAVSAFGYGG TTKPATVTDG ATTTLNVALT AVASVNVTGA VTDGSGHGWP LYAKVTVTGV
     SGVYDYTTPA NGRYSIKLPA GQTYTLTYES QYPGYQTVTK EVVVGSRNVT ANVAVPVNTT
     TCTTAPGYTF GSDGEYETFD GATVPAGWSV VDNKGNGQGW KFTDDGNRGN LTGGTGNFAV
     VDSDAYGAGG SQDTSLVSPV VNLTDVTAPV VRFNQDFNQL ADDTGDVDLS IDGGATWTNV
     LRQETDVRGP KVTEIPIPQA AGKAQVQVRF HYYDASYEWW WEVDNVLIGS QVTCVPVDGG
     LVVGHVRDKN DSSYVNGATV TSADRPSESA VTVATPDDPG LADGFYWLYS TLTDTHKFTA
     KAGNYVSQSK QVDVQADWAT AANFQLAAGR LSVTPAQVSA TVQMPSGKAS RTFTVTNTGG
     APVEVEFSER DNGFELLRAD GSRMTRQQVL GATGAPEQRL TVPTSFAAKA SGRAAMAAPA
     AVTPQAAPWT DITDYPANIM DNRVVSLDGK VYSIGGGDGS SSTTKNYAYD AVAQTWTAIA
     DLPGARNALA VGVVDGKIIA TGGWADGGPD AATWSYDPAA NTWTELADNP APRAAAGQAV
     VDGKLYAIGG CTTAACTPMS NTVVRYDPGS DTWETMANYP KSVAFASCGG IDGTIYCTGG
     NDGAAAQKAS YAFDPGANTW TAIADAPVDN WASSFAVASG KLLVVGGSQG GAISNAGFAY
     DPATSSWSNL PNANTARYRG GAACGFYKIG GSSGSFSAAP DSEVLPGFEG CAEAAADVSW
     MTIDKSAVTL TPGQKVTVTV GMTANVDQPG TYSGSVGIKE NTPYTVAPVA VTMTATPPKT
     WGKLMGTVTG TSCQGATSPI AGAVVQVDSW AMSWTFATDT QGKYAYWVDR RNNPLTMIVA
     KDGWKPQTRQ TRIDTTTPTV ENFGLSPIRC
//