ID   V7J3U2_MYCAV            Unreviewed;       560 AA.
AC   V7J3U2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Peptidase S8 {ECO:0000313|EMBL:ETA92256.1};
GN   ORFNames=O982_24135 {ECO:0000313|EMBL:ETA92256.1};
OS   Mycobacterium avium 10-5581.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1392000 {ECO:0000313|EMBL:ETA92256.1, ECO:0000313|Proteomes:UP000018557};
RN   [1] {ECO:0000313|EMBL:ETA92256.1, ECO:0000313|Proteomes:UP000018557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10-5581 {ECO:0000313|EMBL:ETA92256.1,
RC   ECO:0000313|Proteomes:UP000018557};
RA   Bannantine J.P., Robbe-Austerman S., O'Connell C.;
RT   "Genome sequence of MAC strains.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-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:ETA92256.1}.
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DR   EMBL; AYNT01000252; ETA92256.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7J3U2; -.
DR   MEROPS; S08.131; -.
DR   PATRIC; fig|1392000.4.peg.5149; -.
DR   Proteomes; UP000018557; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR023834; T7SS_pept_S8A_mycosin.
DR   NCBIfam; TIGR03921; T7SS_mycosin; 1.
DR   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF00082; Peptidase_S8; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..560
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004761690"
FT   TRANSMEM        529..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..137
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          240..488
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          14..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..187
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..238
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        90
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        122
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        441
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   560 AA;  56876 MW;  93DDF5D5086585E9 CRC64;
     MSAAAVMGLT GLWGAPPAAA VEPPQIDVGA TPPDGPPGPD QPMRQGAFCP KVGTLPGTDY
     RVQPHNLDML DLGEAWRFGR GAGQKVAVID TGVSPHPRLT DLVAGGDYVV AGGDGLADCD
     AHGTIVASLI AAQPADGKTP LPPARQGRRP DTVPTTEAPP PPPPPQTVTV QLPPPPPPPP
     PPDGAGWRPR HLPQVVVPAG HTKLAPEGPG SGPDDPAPPG PAEPSPPPPG PPPPVAPAAD
     GFSGVAPDVE VIAIRQSSKA FSPKDAFAGN QDPATRRKAG DIRTMARAIV HAANMGATVI
     NISEVSCMTA TDMIDQRDLG AAIHYAAVDR NAVIVAAAGN VGNESGNDCK QNPIYNPLTP
     NDPRDWAGVT TVATPAWFSD YVLTVGAVDS TGAPLDSSMA GPWVSIAAPG TDVESLSPRD
     DGLMNAVEGN KNTLVPQAGT SFSAALVSGV AALVRAKYPQ LTAHQVINRL LATARAPARG
     VDNQVGHGIV DPVAALTYDL PPGEPVGPQR LAAPLVLAPP KVGRDMTPVW VAAAGVGGLA
     LLCSVVLGSA ALMRRRGQGS
//