ID   A0A3N1Q8X5_9MICO        Unreviewed;      1114 AA.
AC   A0A3N1Q8X5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=PA domain-containing protein {ECO:0000313|EMBL:ROQ37139.1};
GN   ORFNames=EDF46_2588 {ECO:0000313|EMBL:ROQ37139.1};
OS   Frondihabitans sp. PhB188.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frondihabitans.
OX   NCBI_TaxID=2485200 {ECO:0000313|EMBL:ROQ37139.1, ECO:0000313|Proteomes:UP000269803};
RN   [1] {ECO:0000313|EMBL:ROQ37139.1, ECO:0000313|Proteomes:UP000269803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PhB188 {ECO:0000313|EMBL:ROQ37139.1,
RC   ECO:0000313|Proteomes:UP000269803};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (NOV-2018) 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:ROQ37139.1}.
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DR   EMBL; RJUO01000004; ROQ37139.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1Q8X5; -.
DR   OrthoDB; 9813435at2; -.
DR   Proteomes; UP000269803; 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; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
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; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034213; S8_Vpr-like.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000269803};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..1114
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018136200"
FT   DOMAIN          196..666
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          467..549
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   REGION          257..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        282
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        628
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1114 AA;  112930 MW;  20574B54B2CE172C CRC64;
     MPRSSSRPIR KVALASVAAA ALVAASLATT SQIATASTSP GSLTSLAPAL KLNARLDKAT
     GKVAVFVRTE GAGALSVDAT AKGGSLSGRP QSSAAKNRVA DIRRTNSAVT KAIASADPAV
     TTLYTTAYTV PGVAVIADAS VLKAIAARSD VVSISPITQR SVPKPVTTKG EEAPLNSNDA
     IYTRTLNAWQ QTGHTGTGIN IAVIDTGLDY THADFGGPGT TAAYDEALAS TAAPASSLYD
     SAKFLGGTDF AGATYNADPD SDAYDPDPAP DANPIDGRGG GHGSHVAGTA AGFGENADKT
     TFTGDYGDLT TDSVNDMYIG PGSAPNSGLY SLKVFGDGGG STDLTGAALD WVGQALTQGK
     NINVVNMSLG SDYSNPDDPD NAKVDALVAR GVLPVMSAGN SGDFTDVGGS PANSENGLSV
     AAASSGSAVY DGIDVTAPAG ISGTYNAQYS IAYTKPLTLR ADVFVPSAAG STGCAPFSSD
     DAARIAGKIV LLHWNDAALE CGSVTRFTNA TNAGAAGVLL GGSVNVFDAG ISGNADIPGA
     EITKDAYAAI LRTVDGGDTV TVSFKDSLRL YKSEIVPSLT DTLATFSSRG VHGSYDKIVK
     PDVAAPGVNV LSVLSGAGTG RTSESGTSMA SPDAAGIAAL VFEAHDGWTA KQVKADIMNT
     ATHDLKDADG NLYSTISQGT GRIDALQAVT NQVTVRSDEN EGLITASYGA VAVSKPLTAK
     RTLVLHNSGN TSQTYSVAYA SRIAAPGVTF TVSASTVVVP ARGDVTVTLT MKIPDPKALR
     KVIDPTQNAT AGVGDAEIVR DFVASATGSV QFTPADSTRS PLRLSVFAAP KPISANTGAT
     AVFAKKTSTT AVLGISGTTL KQGTGVQAYT GLTAAFVLGA TSPVKTFPAG SPQQSLAGAD
     LIAVGAASTA PLEKDRSDGI LSFGVKTNGP IANPGVDGAP EVYIDTDGDG EADFVTYVTK
     STTADATFVT TIDLVSGKAV DVEPFNADYA GVDVNTFDSS VAVLPVSLKA LGFTSKSKKT
     SITYEVATES AYAPGLASTG SYVVDQTNAA TFDVFAPSLW FSQKKSDDLG GVLLRDQSPG
     IAVHRTTAST KRILLLHLHN SVSKQSQIVS QKTK
//