ID   A0A285VIC5_9MICO        Unreviewed;      1113 AA.
AC   A0A285VIC5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=PA domain-containing protein {ECO:0000313|EMBL:SOC53743.1};
GN   ORFNames=SAMN05421879_102102 {ECO:0000313|EMBL:SOC53743.1};
OS   Ornithinimicrobium cerasi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Ornithinimicrobiaceae; Ornithinimicrobium.
OX   NCBI_TaxID=2248773 {ECO:0000313|EMBL:SOC53743.1, ECO:0000313|Proteomes:UP000219688};
RN   [1] {ECO:0000313|Proteomes:UP000219688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA17B2 {ECO:0000313|Proteomes:UP000219688};
RA   Varghese N., Submissions S.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; OBQK01000002; SOC53743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285VIC5; -.
DR   Proteomes; UP000219688; 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   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 2.60.40.2310; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; IPR034197; Peptidases_S8_3.
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; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
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:UP000219688};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1113
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038706922"
FT   DOMAIN          210..650
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          473..530
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          701..783
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        219
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        299
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        614
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1113 AA;  113608 MW;  AFB655E3E2962A9B CRC64;
     MTRVRAPRRL ALLLAGTLAL TMASAPAGSA TDPPAPPDDW TATALTPDGP VIHAPLSASG
     AMATSDEDLL ARTDAEVVPV MVKLDLDGAA SYAGGKDGLA PTSPQVTGRA LADNAAAVEP
     YLAHAEEVTA EAATAVVGSV PAAVVTGSYE VAYGGLSALV PANRAKDLLK VPGVVAVQAD
     EAREIQTDAS PEFIGATEVW PSLGGSSTAG EGVVVGVLDS GIWPEHPSFL DPGIDRPDVG
     ELGCEFGDGT DPALGDAFEC NDKMLGAYAF LDTNVLVTGD IADDYCSGTE CTARDDNGHG
     THTASTAAGS PVEEAVVLGV DRGPVSGIAP GASVVMYRVC RPSCYSSDSV NAVQQAIIDG
     VDVLNFSISG GSDPYNDPVE LSFLDATAAG ISVNASAGNN GPAAATANHA GPWVTTVAAS
     TSDRHFRTDV VLTADNGDTY TKVGDTVTDG ITDTEVIHVT EVTPADPLCL TPLPEGSVAG
     KVVVCDRGVN ARVDKGYNVL QGGAAGMILL NLVTQGTQTD NHWLPTAHLD GPNDEFKDFL
     ATHTGVTASW GAGEPREVRG DVMAGFSSRG PLGPVLKPDV TAPGVQILAG HTPTPNTISS
     GPPGELFQAI AGTSMSSPHA AGSAALLTAA HPDWSPSEIK SALMMTSVQD VLEEDGVTAT
     DPFDRGAGSI RVDRAADPTL VMDVSAEDFY AAAAGSLEAV DLNLASIYVD PLPGLVTLER
     TVRNVSGQTQ RFDALVSADP GVVVSVSPKN PVVEAGASLT LTVTIDTTAA DAGWRFGQIT
     LAPKARGYAA AVLPLAVNAV DGDLRLTHSC EPTEITRSGL AECTATLTNL GASDAEVTAS
     LTAPKKVVIS DVSAPATPTS DGWVFEGTIA GALAPTIDSI TEGGLFGYVP LASFGIAPIA
     GVGDESIVNY NVPAFQFGSE TYTRLGVTSN GYAVVGGGSG SDVQFDPPGI PDGAAPNNVL
     APLWTDLNPA DGGALRIATL GDGVSTWLVT EWSEVPAYGT TQANSFQTWI LLGGTEEVTF
     AYGTVQGTGP NAWQMGAENR DGSSGATLPL TDPVDATDTD WTVNTSPPVA GEELTITYSA
     SSRFVGTYPL RLEVSTPDRR TTIADVVNLV VVR
//