MYCP2_MYCTU
ID MYCP2_MYCTU Reviewed; 550 AA.
AC O05458; F2GDP7; I6YHE0; L0TH18;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Mycosin-2 {ECO:0000303|PubMed:10974545};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:O05461};
DE AltName: Full=MycP2 protease {ECO:0000305};
DE Flags: Precursor;
GN Name=mycP2 {ECO:0000303|PubMed:10974545};
GN OrderedLocusNames=Rv3886c {ECO:0000312|EMBL:CCP46715.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=H37Rv;
RX PubMed=10974545; DOI=10.1016/s0378-1119(00)00277-8;
RA Brown G.D., Dave J.A., Gey van Pittius N.C., Stevens L., Ehlers M.R.,
RA Beyers A.D.;
RT "The mycosins of Mycobacterium tuberculosis H37Rv: a family of subtilisin-
RT like serine proteases.";
RL Gene 254:147-155(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10974545};
CC Single-pass membrane protein {ECO:0000255}. Note=Cell wall-associated.
CC {ECO:0000269|PubMed:10974545}.
CC -!- INDUCTION: Constitutively expressed during growth in culture.
CC {ECO:0000269|PubMed:10974545}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46715.1; -; Genomic_DNA.
DR RefSeq; NP_218403.1; NC_000962.3.
DR RefSeq; WP_003400012.1; NZ_KK339374.1.
DR AlphaFoldDB; O05458; -.
DR SMR; O05458; -.
DR STRING; 83332.Rv3886c; -.
DR MEROPS; S08.131; -.
DR PaxDb; O05458; -.
DR PRIDE; O05458; -.
DR GeneID; 45427889; -.
DR GeneID; 886215; -.
DR KEGG; mtu:Rv3886c; -.
DR PATRIC; fig|83332.111.peg.4327; -.
DR TubercuList; Rv3886c; -.
DR eggNOG; COG1404; Bacteria.
DR OMA; HQVINRI; -.
DR PhylomeDB; O05458; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR Gene3D; 3.40.50.200; -; 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; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR023834; T7SS_pept_S8A_mycosin.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR TIGRFAMs; TIGR03921; T7SS_mycosin; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..550
FT /note="Mycosin-2"
FT /id="PRO_5004157025"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 79..490
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 34..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 103
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 435
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 550 AA; 55594 MW; 0197C3F47ADDF150 CRC64;
MASPLNRPGL RAAAASAALT LVALSANVPA AQAIPPPSVD PAMVPADARP GPDQPMRRSN
SCSTPITVRN PDVAQLAPGF NLVNISKAWQ YSTGNGVPVA VIDTGVSPNP RLPVVPGGDY
IMGEDGLSDC DAHGTVVSSI IAAAPLGILP MPRAMPATAA FPPPAGPPPV TAAPAPPVEV
PPPMPPPPPV TITQTVAPPP PPPEDAGAMA PSNGPPDPQT EDEPAVPPPP PGAPDGVVGV
APHATIISIR QSSRAFEPVN PSSAGPNSDE KVKAGTLDSV ARAVVHAANM GAKVINISVT
ACLPAAAPGD QRVLGAALWY AATVKDAVIV AAAGNDGEAG CGNNPMYDPL DPSDPRDWHQ
VTVVSSPSWF SDYVLSVGAV DAYGAALDKS MSGPWVGVAA PGTHIMGLSP QGGGPVNAYP
PSRPGEKNMP FWGTSFSAAY VSGVAALVRA KFPELTAYQV INRIVQSAHN PPAGVDNKLG
YGLVDPVAAL TFNIPSGDRM APGAQSRVIT PAAPPPPPDH RARNIAIGFV GAVATGVLAM
AIGARLRRAR
