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Database: UniProt
Entry: O06316_MYCTO
LinkDB: O06316_MYCTO
Original site: O06316_MYCTO 
ID   O06316_MYCTO            Unreviewed;       455 AA.
AC   O06316; F2GIK3; Q7D5I8;
DT   01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:AAK47895.1};
GN   OrderedLocusNames=MT3555 {ECO:0000313|EMBL:AAK47895.1};
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331 {ECO:0000313|EMBL:AAK47895.1, ECO:0000313|Proteomes:UP000001020};
RN   [1] {ECO:0000313|EMBL:AAK47895.1, ECO:0000313|Proteomes:UP000001020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh {ECO:0000313|Proteomes:UP000001020};
RX   PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J., DeBoy R., Dodson R., Gwinn M., Haft D., Hickey E.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M., Salzberg S.L.,
RA   Delcher A., Utterback T., Weidman J., Khouri H., Gill J., Mikula A.,
RA   Bishai W., Jacobs Jr W.R.Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; AE000516; AAK47895.1; -; Genomic_DNA.
DR   PIR; F70564; F70564.
DR   RefSeq; WP_003418331.1; NZ_KK341227.1.
DR   AlphaFoldDB; O06316; -.
DR   SMR; O06316; -.
DR   MEROPS; S08.131; -.
DR   KEGG; mtc:MT3555; -.
DR   PATRIC; fig|83331.31.peg.3814; -.
DR   HOGENOM; CLU_011263_13_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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; 1.
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; 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; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000001020};
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..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..455
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004156817"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..376
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          389..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        98
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        129
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        329
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   455 AA;  46016 MW;  7DC901D25C07C8A8 CRC64;
     MTTSRTLRLL VVSALATLSG LGTPVAHAVS PPPIDERWLP ESALPAPPRP TVQREVCTEV
     TAESGRAFGR AERSAQLADL DQVWRLTRGA GQRVAVIDTG VARHRRLPKV VAGGDYVFTG
     DGTADCDAHG TLVAGIIAAA PDAQSDNFSG VAPDVTLISI RQSSSKFAPV GDPSSTGVGD
     VDTMAKAVRT AADLGASVIN ISSIACVPAA AAPDDRALGA ALAYAVDVKN AVIVAAAGNT
     GGAAQCPPQA PGVTRDSVTV AVSPAWYDDY VLTVGSVNAQ GEPSAFTLAG PWVDVAATGE
     AVTSLSPFGD GTVNRLGGQH GSIPISGTSY AAPVVSGLAA LIRARFPTLT ARQVMQRIES
     TAHHPPAGWD PLVGNGTVDA LAAVSSDSIP QAGTATSDPA PVAVPVPRRS TPGPSDRRAL
     HTAFAGAAIC LLALMATLAT ASRRLRPGRN GIAGD
//
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